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3DR3

Structure of IDP00107, a potential N-acetyl-gamma-glutamylphosphate reductase from Shigella flexneri

Functional Information from GO Data
ChainGOidnamespacecontents
A0003942molecular_functionN-acetyl-gamma-glutamyl-phosphate reductase activity
A0005737cellular_componentcytoplasm
A0006526biological_processarginine biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
A0051287molecular_functionNAD binding
A0070401molecular_functionNADP+ binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NA A 335
ChainResidue
AASN22
AHIS24
AMET27
AHOH448

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NA A 336
ChainResidue
ATYR264
ALYS267
AHOH426

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR RESIDUE MLT A 337
ChainResidue
ACYS200
APRO236
AARG237
ALYS281
AASN282
ALEU309
AHOH363
AHOH457
AHOH489
AHOH601
AHOH703
ATYR12
AGLN51

Functional Information from PROSITE/UniProt
site_idPS00142
Number of Residues10
DetailsZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. ATAHEVSHDL
ChainResidueDetails
AALA79-LEU88

site_idPS01224
Number of Residues17
DetailsARGC N-acetyl-gamma-glutamyl-phosphate reductase active site. IAvPGCYPTAaqlALkP
ChainResidueDetails
AILE149-PRO165

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00150
ChainResidueDetails
ACYS154

223166

PDB entries from 2024-07-31

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