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3FNG

Crystal structure of InhA bound to triclosan derivative

Functional Information from GO Data
ChainGOidnamespacecontents
A0004318molecular_functionenoyl-[acyl-carrier-protein] reductase (NADH) activity
A0005504molecular_functionfatty acid binding
A0005886cellular_componentplasma membrane
A0006633biological_processfatty acid biosynthetic process
A0009274cellular_componentpeptidoglycan-based cell wall
A0016491molecular_functionoxidoreductase activity
A0030497biological_processfatty acid elongation
A0046677biological_processresponse to antibiotic
A0050343molecular_functiontrans-2-enoyl-CoA reductase (NADH) activity
A0070403molecular_functionNAD+ binding
A0071768biological_processmycolic acid biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues31
DetailsBINDING SITE FOR RESIDUE NAD A 300
ChainResidue
AGLY14
ASER94
AILE95
AGLY96
AILE122
AMET147
AASP148
APHE149
ALYS165
AALA191
AGLY192
AILE15
APRO193
AILE194
ATHR196
AALA198
AHOH273
AHOH275
AHOH301
AHOH307
AHOH345
AHOH349
AILE16
AJPL400
AHOH430
ASER20
AILE21
APHE41
ALEU63
AASP64
AVAL65

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE JPL A 400
ChainResidue
AGLY96
AMET98
APHE149
ATYR158
AALA198
AMET199
ANAD300

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:10336454, ECO:0000269|PubMed:16647717, ECO:0000269|PubMed:7886450, ECO:0007744|PDB:1BVR, ECO:0007744|PDB:1ENY, ECO:0007744|PDB:2AQ8
ChainResidueDetails
ASER20
AASP64
AILE95
ALYS165
AILE194

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10336454
ChainResidueDetails
ATYR158

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: May act as an intermediate that passes the hydride ion from NADH to the substrate => ECO:0000305|PubMed:10336454
ChainResidueDetails
APHE149

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer => ECO:0000305|PubMed:10521269
ChainResidueDetails
ATYR158

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:20864541, ECO:0000269|PubMed:21143326
ChainResidueDetails
ATHR266

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1qsg
ChainResidueDetails
ATYR158
ALYS165

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1qsg
ChainResidueDetails
AMET161
ALYS165

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PDB entries from 2024-07-17

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