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3PJD

Structure of ENR G93A mutant-NAD+-Triclosan complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004318molecular_functionenoyl-[acyl-carrier-protein] reductase (NADH) activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006633biological_processfatty acid biosynthetic process
A0008610biological_processlipid biosynthetic process
A0009102biological_processbiotin biosynthetic process
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0030497biological_processfatty acid elongation
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
A0046677biological_processresponse to antibiotic
A0051289biological_processprotein homotetramerization
A0070404molecular_functionNADH binding
A1902494cellular_componentcatalytic complex
B0004318molecular_functionenoyl-[acyl-carrier-protein] reductase (NADH) activity
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0006633biological_processfatty acid biosynthetic process
B0008610biological_processlipid biosynthetic process
B0009102biological_processbiotin biosynthetic process
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0030497biological_processfatty acid elongation
B0032991cellular_componentprotein-containing complex
B0042802molecular_functionidentical protein binding
B0046677biological_processresponse to antibiotic
B0051289biological_processprotein homotetramerization
B0070404molecular_functionNADH binding
B1902494cellular_componentcatalytic complex
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE NAD A 701
ChainResidue
AGLY13
AALA93
ALEU144
ASER145
ALYS163
AALA189
AGLY190
APRO191
AILE192
ATHR194
AALA196
ASER19
ATCL801
AHOH802
AHOH811
AHOH820
AILE20
AGLN40
ACYS63
AASP64
AVAL65
ASER91
AILE92

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TCL A 801
ChainResidue
AALA93
AALA95
ALEU100
ATYR156
AALA196
AILE200
APHE203
ANAD701

site_idAC3
Number of Residues26
DetailsBINDING SITE FOR RESIDUE NAD B 702
ChainResidue
BGLY13
BALA15
BSER19
BILE20
BGLN40
BCYS63
BASP64
BVAL65
BSER91
BILE92
BALA93
BLEU144
BSER145
BTYR146
BLYS163
BALA189
BGLY190
BPRO191
BILE192
BTHR194
BALA196
BTCL802
BHOH803
BHOH812
BHOH831
BHOH842

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE TCL B 802
ChainResidue
BALA93
BALA95
BTYR146
BTYR156
BALA196
BALA197
BNAD702

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
ATYR146
ATYR156
BTYR146
BTYR156

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:10201369, ECO:0000269|PubMed:10398587, ECO:0000269|PubMed:10493822, ECO:0000269|PubMed:10595560, ECO:0000269|PubMed:11514139, ECO:0000269|PubMed:12109908, ECO:0000269|PubMed:12699381, ECO:0000269|PubMed:8953047
ChainResidueDetails
AGLY13
BGLN40
BASP64
BILE92
BLYS163
BILE192
ASER19
AGLN40
AASP64
AILE92
ALYS163
AILE192
BGLY13
BSER19

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AALA95
BALA95

site_idSWS_FT_FI4
Number of Residues6
DetailsSITE: Involved in acyl-ACP binding
ChainResidueDetails
ALYS201
AARG204
ALYS205
BLYS201
BARG204
BLYS205

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 606
ChainResidueDetails
ATYR156proton acceptor, proton donor
ALYS163electrostatic stabiliser

site_idMCSA2
Number of Residues2
DetailsM-CSA 606
ChainResidueDetails
BTYR156proton acceptor, proton donor
BLYS163electrostatic stabiliser

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PDB entries from 2024-07-10

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