Literature summary for 3.1.21.1 extracted from

Parsiegla, G.; Noguere, C.; Santell, L.; Lazarus, R.A.; Bourne, Y.
The structure of human DNase I bound to magnesium and phosphate ions points to a catalytic mechanism common to members of the DNase I-like superfamily (2012), Biochemistry, 51, 10250-10258.

Crystallization (Commentary)

Crystallization (Comment)	Organism
in complex with magnesium and phosphate ions, both bound in the active site, to 1.95 A resolution. Data suggest a magnesium-assisted pentavalent phosphate transition state during catalysis, where Asp168 may play a key role as a general catalytic base. Residue Asn7 plays a critical role in the catalytic mechanism, participating indirectly in the coordination sphere of the Mg2+ ion with an H-bond of its amide oxygen with a coordinated water molecule and connects Asp168 and Glu39 with an H-bonding network via its amide nitrogen	Homo sapiens

Crystallization (Comment)

Organism

in complex with magnesium and phosphate ions, both bound in the active site, to 1.95 A resolution. Data suggest a magnesium-assisted pentavalent phosphate transition state during catalysis, where Asp168 may play a key role as a general catalytic base. Residue Asn7 plays a critical role in the catalytic mechanism, participating indirectly in the coordination sphere of the Mg2+ ion with an H-bond of its amide oxygen with a coordinated water molecule and connects Asp168 and Glu39 with an H-bonding network via its amide nitrogen

Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
N7A	complete loss of activity	Homo sapiens
N7S	complete loss of activity	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P24855	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

Synonyms

Synonyms	Comment	Organism
deoxyribonuclease-1	-	Homo sapiens
Dnase1	-	Homo sapiens

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Release 2023.1 (January 2023)