Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7NOT

Crystal structure of Mycobacterium tuberculosis ArgC in complex with nicotinamide adenine dinucleotide phosphate (NADP+) and 5-Methoxy-3-indoleacetic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0003942molecular_functionN-acetyl-gamma-glutamyl-phosphate reductase activity
A0005515molecular_functionprotein binding
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
B0003942molecular_functionN-acetyl-gamma-glutamyl-phosphate reductase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0006526biological_processarginine 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_processarginine 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_processarginine 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
E0003942molecular_functionN-acetyl-gamma-glutamyl-phosphate reductase activity
E0005515molecular_functionprotein binding
E0005737cellular_componentcytoplasm
E0006526biological_processarginine biosynthetic process
E0016491molecular_functionoxidoreductase activity
E0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
E0051287molecular_functionNAD binding
E0070401molecular_functionNADP+ binding
F0003942molecular_functionN-acetyl-gamma-glutamyl-phosphate reductase activity
F0005515molecular_functionprotein binding
F0005737cellular_componentcytoplasm
F0006526biological_processarginine biosynthetic process
F0016491molecular_functionoxidoreductase activity
F0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
F0051287molecular_functionNAD binding
F0070401molecular_functionNADP+ binding
G0003942molecular_functionN-acetyl-gamma-glutamyl-phosphate reductase activity
G0005515molecular_functionprotein binding
G0005737cellular_componentcytoplasm
G0006526biological_processarginine biosynthetic process
G0016491molecular_functionoxidoreductase activity
G0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
G0051287molecular_functionNAD binding
G0070401molecular_functionNADP+ binding
H0003942molecular_functionN-acetyl-gamma-glutamyl-phosphate reductase activity
H0005515molecular_functionprotein binding
H0005737cellular_componentcytoplasm
H0006526biological_processarginine biosynthetic process
H0016491molecular_functionoxidoreductase activity
H0016620molecular_functionoxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
H0051287molecular_functionNAD binding
H0070401molecular_functionNADP+ binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue MYI A 401
ChainResidue
ACYS158
AHOH510
ATYR159
ASER186
AGLY187
AGLY190
AALA191
ATYR211
AHIS217
ALEU243

site_idAC2
Number of Residues7
Detailsbinding site for residue MYI B 401
ChainResidue
BSER186
BGLY187
BGLY190
BALA191
BTYR211
BHIS217
BLEU243

site_idAC3
Number of Residues24
Detailsbinding site for residue NAP C 401
ChainResidue
CGLY16
CSER18
CGLY19
CTYR20
CALA21
CALA47
CALA48
CTHR49
CSER50
CTHR73
CALA87
CLEU88
CPRO89
CHIS92
CCYS109
CGLY110
CSER189
CGLY190
CGLY192
CARG193
CALA194
CASN320
CGLY324
CTHR325

site_idAC4
Number of Residues8
Detailsbinding site for residue MYI C 402
ChainResidue
CTYR159
CSER186
CGLY187
CGLY190
CALA191
CTYR211
CHIS217
CLEU243

site_idAC5
Number of Residues25
Detailsbinding site for residue NAP D 401
ChainResidue
DGLY16
DSER18
DGLY19
DTYR20
DALA21
DALA47
DALA48
DTHR49
DSER50
DTHR73
DALA87
DLEU88
DHIS92
DCYS109
DGLY110
DSER189
DGLY190
DGLY192
DARG193
DALA194
DASN320
DLEU321
DGLY324
DTHR325
DHOH514

site_idAC6
Number of Residues8
Detailsbinding site for residue MYI D 402
ChainResidue
DSER186
DGLY187
DGLY190
DALA191
DTYR211
DHIS217
DHIS219
DLEU243

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 Residues8
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00150
ChainResidueDetails
ACYS158
BCYS158
CCYS158
DCYS158
ECYS158
FCYS158
GCYS158
HCYS158

224572

PDB entries from 2024-09-04

PDB statisticsPDBj update infoContact PDBjnumon