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3FNH

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 Residues24
DetailsBINDING SITE FOR RESIDUE NAD A 300
ChainResidue
AGLY14
ASER94
AILE95
AILE122
AMET147
AASP148
APHE149
AMET161
ALYS165
AGLY192
APRO193
AILE15
AILE194
ATHR196
ALEU197
AALA198
AJPJ400
AILE16
ASER20
AILE21
APHE41
ALEU63
AASP64
AVAL65

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE JPJ A 400
ChainResidue
AGLY96
APHE97
AMET98
APHE149
ATYR158
ALYS165
APRO193
AALA198
AILE202
AILE215
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 2024-11-06

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