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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_functionglutamate N-acetyltransferase activity
A0006526biological_processarginine biosynthetic process
B0004358molecular_functionglutamate N-acetyltransferase activity
B0006526biological_processarginine biosynthetic process
C0004358molecular_functionglutamate N-acetyltransferase activity
C0006526biological_processarginine biosynthetic process
D0004358molecular_functionglutamate N-acetyltransferase activity
D0006526biological_processarginine biosynthetic process
E0004358molecular_functionglutamate N-acetyltransferase activity
E0006526biological_processarginine biosynthetic process
F0004358molecular_functionglutamate N-acetyltransferase activity
F0006526biological_processarginine biosynthetic process
G0004358molecular_functionglutamate N-acetyltransferase activity
G0006526biological_processarginine biosynthetic process
H0004358molecular_functionglutamate N-acetyltransferase activity
H0006526biological_processarginine biosynthetic process
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile
ChainResidueDetails
BAYA181
DAYA181
FAYA181
HAYA181
ETHR148
ELYS170
GTHR148
GLYS170

site_idSWS_FT_FI2
Number of Residues16
DetailsBINDING: BINDING => ECO:0000269|PubMed:21796301
ChainResidueDetails
BAYA181
BGLU260
BASN381
BTHR386
DAYA181
DGLU260
DASN381
DTHR386
FAYA181
FGLU260
FASN381
FTHR386
HAYA181
HGLU260
HASN381
HTHR386

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole
ChainResidueDetails
AGLY112
CGLY112
EGLY112
GGLY112

site_idSWS_FT_FI4
Number of Residues4
DetailsSITE: Cleavage; by autolysis
ChainResidueDetails
AALA180
CALA180
EALA180
GALA180

219869

PDB entries from 2024-05-15

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