Literature summary for 3.4.24.46 extracted from

Gomis-Ruth, F.X.; Kress, L.F.; Kellermann, J.; Mayr, I.; Lee, X.; Huber, R.; Bode, W.
Refined 2.0 A X-ray crystal structure of the snake venom zinc-endopeptidase adamalysin II. Primary and tertiary structure determination, refinement, molecular structure and comparison with astacin, collagenase and thermolysin (1994), J. Mol. Biol., 239, 513-544.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
Crotalus adamanteus	Crotalus adamanteus
structure	Crotalus adamanteus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	metalloproteinase	Crotalus adamanteus
Ca2+	calcium binding site	Crotalus adamanteus
Zn2+	zinc-endopeptidase	Crotalus adamanteus
Zn2+	zinc-binding motif, almost tetrahedrally co-ordinated by His142, His146 and His152 and a water molecule anchored to an intermediate Glu residue, Glu143	Crotalus adamanteus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
additional information	-	amino acid sequence compared to other adamalysins	Crotalus adamanteus
additional information	-	shares a similar overall topology with astacin, with the collagenase catalytic domains and the Pseudomonas aeruginosa alkaline proteinase and exhibits a virtual identical zinc environment with these other metzincins	Crotalus adamanteus
additional information	-	primary and tertiary structure	Crotalus adamanteus

Organism

Organism	UniProt	Comment	Textmining
Crotalus adamanteus	-	Eastern diamondback rattlesnake	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
venom	-	Crotalus adamanteus	-

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Release 2023.1 (January 2023)