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(1S)-2-(1H-indol-3-yl)-1-[5-(2,4,6-trimethylbenzyl)-1,3-thiazol-2-yl]ethanamine
-
(2R)-2-amino-N'-[(E)-(4-hydroxynaphthalen-1-yl)methylidene]-2-phenylacetohydrazide
-
(2S)-2-amino-2-[4-(trifluoromethyl)phenyl]-N'-[(E)-[3-(trifluoromethyl)phenyl]methylidene]acetohydrazide
-
(2S)-2-amino-2-[4-(trifluoromethyl)phenyl]-N'-[(E)-[4-(trifluoromethyl)phenyl]methylidene]acetohydrazide
-
(2S)-2-amino-3-(1H-indol-3-yl)-N'-[(E)-(2,4,6-trimethylphenyl)methylidene]propanehydrazide
-
(2S)-2-amino-3-(1H-indol-3-yl)-N'-[(E)-(2-methylphenyl)methylidene]propanehydrazide
-
(2S)-2-amino-3-(1H-indol-3-yl)-N'-[(E)-phenylmethylidene]propanehydrazide
-
(2S)-2-amino-3-(1H-indol-3-yl)-N'-[(E)-[3-(trifluoromethyl)phenyl]methylidene]propanehydrazide
-
(2S)-2-amino-3-(1H-indol-3-yl)-N'-[(E)-[4-(trifluoromethyl)phenyl]methylidene]propanehydrazide
-
(2S)-2-amino-N'-[(1E)-2-methylbutylidene]-2-[4-(trifluoromethyl)phenyl]acetohydrazide
-
(2S)-2-amino-N'-[(E)-(2,6-dimethylphenyl)methylidene]-3-(1H-indol-3-yl)propanehydrazide
-
(2S)-2-amino-N'-[(E)-(2-bromophenyl)methylidene]-3-(1H-indol-3-yl)propanehydrazide
-
(2S)-2-amino-N'-[(E)-(2-fluorophenyl)methylidene]-3-(1H-indol-3-yl)propanehydrazide
-
(2S)-2-amino-N'-[(E)-(2-hydroxy-3-methylphenyl)methylidene]-2-[4-(trifluoromethyl)phenyl]acetohydrazide
-
(2S)-2-amino-N'-[(E)-(2-hydroxy-3-methylphenyl)methylidene]-3-(1H-indol-3-yl)propanehydrazide
-
(2S)-2-amino-N'-[(E)-(3-methylphenyl)methylidene]-2-[4-(trifluoromethyl)phenyl]acetohydrazide
-
(2S)-2-amino-N'-[(E)-(pyridin-2-yl)methylidene]-2-[4-(trifluoromethyl)phenyl]acetohydrazide
-
(2S)-2-amino-N'-[(E)-cyclohexylmethylidene]-2-[4-(trifluoromethyl)phenyl]acetohydrazide
-
(S)-2-amino-2-(4-(trifluoromethyl)phenyl)acetohydrazide
-
(S)-2-amino-3-(1H-indol-3-yl)propanehydrazide
-
(S)-2-amino-N'-(cyclopentylmethylene)-2-(4-(trifluoromethyl)phenyl)acetohydrazide trifluoro acetic acid
-
(S)-2-amino-N'-benzylidene-2-(4-(trifluoromethyl)phenyl)acetohydrazide
-
1-(4-ethynylphenyl)piperazine
-
1-(4-[1-[2-(4-chlorophenyl)ethyl]-1H-1,2,3-triazol-4-yl]phenyl)piperazine
-
2,6-dimethylbenzaldehyde
-
2-(2,4,6-trimethylphenyl)ethyl L-tryptophanate
-
2-hydroxy-3-methylbenzaldehyde
-
2-[1-[2-(2-fluorophenyl)ethyl]-1H-1,2,3-triazol-4-yl]-1-phenylethan-1-amine
-
3-(trifluoromethyl)benzaldehyde
-
4-(2-[4-[4-(piperazin-1-yl)phenyl]-1H-1,2,3-triazol-1-yl]ethyl)phenol
-
4-(trifluoromethyl)benzaldehyde
-
4-(trifluoromethyl)benzene-1-carboximidamide
-
CP-80,794
-
transition state analogue inhibitor
L363564
-
statine-containing renin inhibitor, hydrogen bonding interaction witht the enzyme, e.g. via Asp32 and Asp215, overview
N',N'''-((1E,1'E)-1,3-phenylenebis(methaneylylidene))bis(2-amino-3-(1H-indol-3-yl)propanehydrazide)
-
N-[2-(2,4,6-trimethylphenyl)ethyl]-L-tryptophanamide
-
Oligopeptide inhibitors
-
PD125967 and PD125754
-
PD-129,541
-
transition state analogue inhibitor
PD-130,328
-
transition state analogue inhibitor
PD-135,040
-
gem-diol inhibitor
rac-(2R,2'R)-N',N'''-((1E,1'E)-1,3-phenylenebis(methaneylylidene))bis(2-amino-3-phenylpropanehydrazide)
-
Synthetic human statine-containing renin inhibitor
-
H-189
-
Synthetic polypeptide inhibitor
-
structure
-
Synthetic renin inhibitor
-
CP-69,799
-
Transition-state isostere inhibitor of renin
-
-
-
H189
-
transition state analogue inhibitor
H256
-
transition state analogue inhibitor
pepstatin
-
-
pepstatin
-
complex formation, structure analysis, conformation changes induced by protein-inhibitor association, proton release and uptake, overview
pepstatin A
-
-
pepstatin A
-
strong inhibition, the inhibitor motif -CH(OH)-CH2- mimicks the tetrahedral intermdiate of the catalytic reaction
additional information
-
cysteine; HgCl2; iodoacetamide; NEM; not: sodium tetrathionate; PCMB; TLCK; TPCK
-
additional information
-
a structural comparison of 21 inhibitor complexes of endothiapepsin; interaction of aspartic proteinases with naturally occuring inhibitors from actinomycetes and Ascaris lumbricoides
-
additional information
-
molecular mechanism of enzyme inhibition by phosphinate and phosphonate inhibitors, molecular dynamic simulations for investigation of the hydrogen bonding pattern, structure, overview
-
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0.1937
(1S)-2-(1H-indol-3-yl)-1-[5-(2,4,6-trimethylbenzyl)-1,3-thiazol-2-yl]ethanamine
Cryphonectria parasitica
pH and temperature not specified in the publication
0.0145
(2R)-2-amino-N'-[(E)-(4-hydroxynaphthalen-1-yl)methylidene]-2-phenylacetohydrazide
Cryphonectria parasitica
pH and temperature not specified in the publication
0.0128
(2S)-2-amino-3-(1H-indol-3-yl)-N'-[(E)-(2,4,6-trimethylphenyl)methylidene]propanehydrazide
Cryphonectria parasitica
pH and temperature not specified in the publication
0.059
(2S)-2-amino-3-(1H-indol-3-yl)-N'-[(E)-(2-methylphenyl)methylidene]propanehydrazide
Cryphonectria parasitica
pH and temperature not specified in the publication
0.049
(2S)-2-amino-3-(1H-indol-3-yl)-N'-[(E)-phenylmethylidene]propanehydrazide
Cryphonectria parasitica
pH and temperature not specified in the publication
0.244
(2S)-2-amino-3-(1H-indol-3-yl)-N'-[(E)-[3-(trifluoromethyl)phenyl]methylidene]propanehydrazide
Cryphonectria parasitica
pH and temperature not specified in the publication
0.007
(2S)-2-amino-3-(1H-indol-3-yl)-N'-[(E)-[4-(trifluoromethyl)phenyl]methylidene]propanehydrazide
Cryphonectria parasitica
pH and temperature not specified in the publication
0.03
(2S)-2-amino-N'-[(E)-(2,6-dimethylphenyl)methylidene]-3-(1H-indol-3-yl)propanehydrazide
Cryphonectria parasitica
pH and temperature not specified in the publication
0.0545
(2S)-2-amino-N'-[(E)-(2-bromophenyl)methylidene]-3-(1H-indol-3-yl)propanehydrazide
Cryphonectria parasitica
pH and temperature not specified in the publication
0.038
(2S)-2-amino-N'-[(E)-(2-fluorophenyl)methylidene]-3-(1H-indol-3-yl)propanehydrazide
Cryphonectria parasitica
pH and temperature not specified in the publication
0.036
(2S)-2-amino-N'-[(E)-(2-hydroxy-3-methylphenyl)methylidene]-3-(1H-indol-3-yl)propanehydrazide
Cryphonectria parasitica
pH and temperature not specified in the publication
0.085
(S)-2-amino-N'-(cyclopentylmethylene)-2-(4-(trifluoromethyl)phenyl)acetohydrazide trifluoro acetic acid
Cryphonectria parasitica
pH and temperature not specified in the publication
0.21
(S)-2-amino-N'-benzylidene-2-(4-(trifluoromethyl)phenyl)acetohydrazide
Cryphonectria parasitica
pH and temperature not specified in the publication
0.142
1-(4-ethynylphenyl)piperazine
Cryphonectria parasitica
pH and temperature not specified in the publication
0.121
1-(4-[1-[2-(4-chlorophenyl)ethyl]-1H-1,2,3-triazol-4-yl]phenyl)piperazine
Cryphonectria parasitica
pH and temperature not specified in the publication
0.0287
2-(2,4,6-trimethylphenyl)ethyl L-tryptophanate
Cryphonectria parasitica
pH and temperature not specified in the publication
0.094
2-[1-[2-(2-fluorophenyl)ethyl]-1H-1,2,3-triazol-4-yl]-1-phenylethan-1-amine
Cryphonectria parasitica
pH and temperature not specified in the publication
0.043
4-(2-[4-[4-(piperazin-1-yl)phenyl]-1H-1,2,3-triazol-1-yl]ethyl)phenol
Cryphonectria parasitica
pH and temperature not specified in the publication
0.0000545
N',N'''-((1E,1'E)-1,3-phenylenebis(methaneylylidene))bis(2-amino-3-(1H-indol-3-yl)propanehydrazide)
Cryphonectria parasitica
pH and temperature not specified in the publication
0.0129
N-[2-(2,4,6-trimethylphenyl)ethyl]-L-tryptophanamide
Cryphonectria parasitica
pH and temperature not specified in the publication
0.0021
rac-(2R,2'R)-N',N'''-((1E,1'E)-1,3-phenylenebis(methaneylylidene))bis(2-amino-3-phenylpropanehydrazide)
Cryphonectria parasitica
pH and temperature not specified in the publication
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complexes of pepstatin A and a statine-containing human renin inhibitor with endothiapepsin
-
crystal structure of enzyme bound to inhibitor Pd130328, inhibitor binding structure and analysis
-
in complex with gem-diol inhibitor PD-135,040, hanging-drop vapour-diffusion method, space group P2(1), unit-cell parameters a : 53.20, b : 73.25, c : 46.00
-
of inhibition of endothiapepsin by cyclohexyl renin inhibitors
-
of the complex between endothiapepsin and an oligopeptide inhibitor
-
sitting drop vapor diffusion method, using 0.1 M NH4Ac, 0.1 M acetate buffer, pH 4.6, and 26% (w/v) PEG 4000
space group P2(1), in complex with H189 unit cell parameters a : 42.48, b : 75.78, c : 42.99, in complex with CP-80,794 unit cell parameters a : 42.55, b : 74.62, c : 44.43, in complex with CP-129,541 unit cell parameters a : 42.47, b : 74.31, c : 42.81, in complex with PD-130,328 unit cell parameters a : 43.88, b : 75.44, c : 43.23, in complex with H256 unit cell parameters a : 43.88, b : 75.44, c : 43.23
-
three-dimensional structure of endothiapepsin complexed with a transition-state isostere inhibitor of renin
-
using ammonium sulfate as precipitant at pH 4.6, X-ray diffraction structure determination and analysis at 2.1 A resolution, multiple isomorphous replacement
-
X-ray crystallographic analysis
-
complexed with H261, crystals grow in two different crystal forms with the same monoclinic sopace group, P2(1), unit cell parameters a : 43.0A, b : 75.7A, c : 42.9A
-
structure studied by neutron crystallography, crystals are monocliic, P2(1), unit cell dimensions a : 43.1 A, b : 75.7 A, c : 42.9 A, endothiapepsin-H261 complex
-
-
-
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Subramanian, E.; Swan, I.D.A.; Liu, M.; Davies, D.R.; Jenkins, J.A.; Tickle, I.J.; Blundell, T.L.
Homology among acid proteases: comparison of crystal structures at 3A resolution of acid proteases from Rhizopus chinensis and Endothia parasitica
Proc. Natl. Acad. Sci. USA
74
556-559
1977
Cryphonectria parasitica
brenda
Whitaker, J.R.
Protease of Endothia parasitica
Methods Enzymol.
19
436-445
1970
Cryphonectria parasitica
-
brenda
Williams, D.C.; Whitaker, J.R.; Caldwell, P.V.
Hydrolysis of peptide bonds of the oxidized B-chain of insulin by Endothia parasitica protease
Arch. Biochem. Biophys.
149
52-61
1972
Cryphonectria parasitica
brenda
Barkholt, V.
Amino acid sequence of endothiapepsin. Complete primary structure of the aspartic protease from Endothia parasitica
Eur. J. Biochem.
167
327-338
1987
Cryphonectria parasitica
brenda
Cooper, J.; Foundling, S.; Hemmings, A.; Blundell, T.; Jones, D.M.; Hallett, A.; Szelke, M.
The structure of a synthetic pepsin inhibitor complexed with endothiapepsin
Eur. J. Biochem.
169
215-221
1987
Cryphonectria parasitica
brenda
Brown, E.D.; Wynne, M.G.; Clarke, A.J.; Yada, R.Y.
Purification of two fungal aspartic proteinases using fast protein liquid chromatography
Agric. Biol. Chem.
54
1563-1565
1990
Cryphonectria parasitica
-
brenda
Cooper, J.; Quail, W.; Frazao, C.; Foundling, S.I.; Blundell, T.L.; Humblet, C.; Lunney, E.A.; Lowther, W.T.; Dunn, B.M.
X-ray crystallographic analysis of inhibition of endothiapepsin by cyclohexyl renin inhibitors
Biochemistry
31
8142-8150
1992
Cryphonectria parasitica
brenda
Bailey, D.; Cooper, J.B.; Veerapandian, B.; Blundell, T.L.; Atrash, B.; Jones, D.M.; Szelke, M.
X-ray-crystallographic studies of complexes of pepstatin A and a statine-containing human renin inhibitor with endothiapepsin
Biochem. J.
289
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1993
Cryphonectria parasitica
brenda
Veerapandian, B.; Cooper, J.B.; Sali, A.; Blundell, T.L.
X-ray analyses of aspartic proteinases. III. Three-dimensional structure of endothiapepsin complexed with a transition-state isostere inhibitor of renin at 1.6 A resolution
J. Mol. Biol.
216
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1990
Cryphonectria parasitica
brenda
Sali, A.; Veerapandian, B.; Cooper, J.B.; Foundling, S.I.; Hoover, D.J.; Blundell, T.L.
High-resolution X-ray diffraction study of the complex between endothiapepsin and an oligopeptide inhibitor: the analysis of the inhibitor binding and description of the rigid body shift in the enzyme
EMBO J.
8
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1989
Cryphonectria parasitica
brenda
Bailey, D.; Cooper, J.B.
A structural comparison of 21 inhibitor complexes of the aspartic proteinase from Endothia parasitica
Protein Sci.
3
2129-2143
1994
Cryphonectria parasitica
brenda
Valler, M.J.; Kay, J.; Aoyagi, T.; Dunn, B.M.
The interaction of aspartic proteinases with naturally-occurring inhibitors from actinomycetes and Ascaris lumbricoides
J. Enzyme Inhib.
1
77-82
1985
Cryphonectria parasitica
brenda
Cooper, J.B.; Myles, D.A.
A preliminary neutron Laue diffraction study of the aspartic proteinase endothiapepsin
Acta Crystallogr. Sect. D
56
246-248
2000
Endothia sp.
-
brenda
Coates, L.; Erskine, P.T.; Mall, S.; Williams, P.A.; Gill, R.S.; Wood, S.P.; Cooper, J.B.
The structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 at 1.37 A
Acta Crystallogr. Sect. D
59
978-981
2003
Cryphonectria parasitica
brenda
Coates, L.; Erskine, P.T.; Wood, S.P.; Myles, D.A.; Cooper, J.B.
A neutron Laue diffraction study of endothiapepsin: implications for the aspartic proteinase mechanism
Biochemistry
40
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2001
Endothia sp.
brenda
Coates, L.; Erskine, P.T.; Crump, M.P.; Wood, S.P.; Cooper, J.B.
Five atomic resolution structures of endothiapepsin inhibitor complexes: implications for the aspartic proteinase mechanism
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318
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2002
Cryphonectria parasitica
brenda
Stultz, C.M.; Karplus, M.
Dynamic ligand design and combinatorial optimization: designing inhibitors to endothiapepsin
Proteins
40
258-289
2000
Endothia sp.
brenda
Cooper, J.B.
Endothiapepsin
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
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2004
Cryphonectria parasitica
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brenda
Vidossich, P.; Carloni, P.
Binding of phosphinate and phosphonate inhibitors to aspartic proteases: a first-principles study
J. Phys. Chem. B
110
1437-1442
2006
Cryphonectria parasitica
brenda
Alexov, E.
Calculating proton uptake/release and binding free energy taking into account ionization and conformation changes induced by protein-inhibitor association: application to plasmepsin, cathepsin D and endothiapepsin-pepstatin complexes
Proteins
56
572-584
2004
Cryphonectria parasitica
brenda
Coates, L.; Erskine, P.T.; Mall, S.; Gill, R.; Wood, S.P.; Myles, D.A.; Cooper, J.B.
X-ray, neutron and NMR studies of the catalytic mechanism of aspartic proteinases
Eur. Biophys. J.
35
559-566
2006
Cryphonectria parasitica
brenda
Koester, H.; Craan, T.; Brass, S.; Herhaus, C.; Zentgraf, M.; Neumann, L.; Heine, A.; Klebe, G.
A small nonrule of 3 compatible fragment library provides high hit rate of endothiapepsin crystal structures with various fragment chemotypes
J. Med. Chem.
54
7784-7796
2011
Cryphonectria parasitica (P11838)
brenda
Mondal, M.; Radeva, N.; Fanlo-Virgos, H.; Otto, S.; Klebe, G.; Hirsch, A.K.
Fragment linking and optimization of inhibitors of the aspartic protease endothiapepsin fragment-based drug design facilitated by dynamic combinatorial chemistry
Angew. Chem. Int. Ed. Engl.
55
9422-9426
2016
Cryphonectria parasitica (P11838)
brenda
Mondal, M.; Unver, M.Y.; Pal, A.; Bakker, M.; Berrier, S.P.; Hirsch, A.K.
Fragment-based drug design facilitated by protein-templated click chemistry fragment linking and optimization of inhibitors of the aspartic protease endothiapepsin
Chemistry
22
14826-14830
2016
Cryphonectria parasitica (P11838)
brenda
Jumde, V.R.; Mondal, M.; Gierse, R.M.; Unver, M.Y.; Magari, F.; van Lier, R.C.W.; Heine, A.; Klebe, G.; Hirsch, A.K.H.
Design and synthesis of bioisosteres of acylhydrazones as stable inhibitors of the aspartic protease endothiapepsin
ChemMedChem
13
2266-2270
2018
Cryphonectria parasitica (P11838)
brenda
Hartman, A.M.; Mondal, M.; Radeva, N.; Klebe, G.; Hirsch, A.K.
Structure-based optimization of inhibitors of the aspartic protease endothiapepsin
Int. J. Mol. Sci.
16
19184-19194
2015
Cryphonectria parasitica (P11838)
brenda
Radeva, N.; Krimmer, S.G.; Stieler, M.; Fu, K.; Wang, X.; Ehrmann, F.R.; Metz, A.; Huschmann, F.U.; Weiss, M.S.; Mueller, U.; Schiebel, J.; Heine, A.; Klebe, G.
Experimental active-site mapping by fragments hot spots remote from the catalytic center of endothiapepsin
J. Med. Chem.
59
7561-7575
2016
Cryphonectria parasitica (P11838)
brenda
Radeva, N.; Schiebel, J.; Wang, X.; Krimmer, S.G.; Fu, K.; Stieler, M.; Ehrmann, F.R.; Metz, A.; Rickmeyer, T.; Betz, M.; Winquist, J.; Park, A.Y.; Huschmann, F.U.; Weiss, M.S.; Mueller, U.; Heine, A.; Klebe, G.
Active site mapping of an aspartic protease by multiple fragment crystal structures versatile warheads to address a catalytic dyad
J. Med. Chem.
59
9743-9759
2016
Cryphonectria parasitica (P11838)
brenda
Mondal, M.; Groothuis, D.; Hirsch, A.
Fragment growing exploiting dynamic combinatorial chemistry of inhibitors of the aspartic protease endothiapepsin
MedChemComm
6
1267-1271
2015
Cryphonectria parasitica (P11838)
-
brenda