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2I3A

Crystal structure of N-Acetyl-gamma-Glutamyl-Phosphate Reductase (Rv1652) from Mycobacterium tuberculosis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003942molecular_functionN-acetyl-gamma-glutamyl-phosphate reductase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0006526biological_processL-arginine 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
B0003942molecular_functionN-acetyl-gamma-glutamyl-phosphate reductase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0006526biological_processL-arginine biosynthetic process
B0016491molecular_functionoxidoreductase activity
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
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0006526biological_processL-arginine biosynthetic process
C0016491molecular_functionoxidoreductase activity
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
D0005515molecular_functionprotein binding
D0005737cellular_componentcytoplasm
D0006526biological_processL-arginine biosynthetic process
D0016491molecular_functionoxidoreductase activity
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 PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BTB A 1400
ChainResidue
AHIS32
AALA34
AASP37
AARG39
ATRP339
APRO340
AASP343

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE BTB B 1500
ChainResidue
BASP37
BARG39
BTRP339
BPRO340
BASP343
BHIS32
BALA34

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BTB C 1600
ChainResidue
CHIS32
CALA34
CASP37
CARG39
CTRP339
CASP343

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BTB D 1700
ChainResidue
DHIS32
DALA34
DASP37
DARG39
DASP343

Functional Information from PROSITE/UniProt
site_idPS01224
Number of Residues17
DetailsARGC N-acetyl-gamma-glutamyl-phosphate reductase active site. IAvPGCYPTAallALfP
ChainResidueDetails
AILE153-PRO169

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00150
ChainResidueDetails
ACYS158
BCYS158
CCYS158
DCYS158

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PDB entries from 2024-10-09

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