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2V4I

Structure of a novel N-acyl-enzyme intermediate of an N-terminal nucleophile (Ntn) hydrolase, OAT2

Functional Information from GO Data
ChainGOidnamespacecontents
A0004358molecular_functionL-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor
A0006526biological_processL-arginine biosynthetic process
B0004358molecular_functionL-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor
B0006526biological_processL-arginine biosynthetic process
C0004358molecular_functionL-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor
C0006526biological_processL-arginine biosynthetic process
D0004358molecular_functionL-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor
D0006526biological_processL-arginine biosynthetic process
E0004358molecular_functionL-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor
E0006526biological_processL-arginine biosynthetic process
F0004358molecular_functionL-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor
F0006526biological_processL-arginine biosynthetic process
G0004358molecular_functionL-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor
G0006526biological_processL-arginine biosynthetic process
H0004358molecular_functionL-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor
H0006526biological_processL-arginine biosynthetic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsSite: {"description":"Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsSite: {"description":"Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21796301","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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