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2CVO

Crystal structure of putative N-acetyl-gamma-glutamyl-phosphate reductase (AK071544) from rice (Oryza sativa)

Functional Information from GO Data
ChainGOidnamespacecontents
A0003942molecular_functionN-acetyl-gamma-glutamyl-phosphate reductase activity
A0006526biological_processL-arginine biosynthetic process
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0051287molecular_functionNAD binding
A0070401molecular_functionNADP+ binding
B0003942molecular_functionN-acetyl-gamma-glutamyl-phosphate reductase activity
B0006526biological_processL-arginine biosynthetic process
B0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
B0051287molecular_functionNAD binding
B0070401molecular_functionNADP+ binding
C0003942molecular_functionN-acetyl-gamma-glutamyl-phosphate reductase activity
C0006526biological_processL-arginine biosynthetic process
C0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
C0051287molecular_functionNAD binding
C0070401molecular_functionNADP+ binding
D0003942molecular_functionN-acetyl-gamma-glutamyl-phosphate reductase activity
D0006526biological_processL-arginine biosynthetic process
D0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
D0051287molecular_functionNAD binding
D0070401molecular_functionNADP+ binding
Functional Information from PROSITE/UniProt
site_idPS01224
Number of Residues17
DetailsARGC N-acetyl-gamma-glutamyl-phosphate reductase active site. VAnPGCYPTSiqlPLvP
ChainResidueDetails
AVAL214-PRO230

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
ACYS219
BCYS219
CCYS219
DCYS219

237735

PDB entries from 2025-06-18

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