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3PJF

Structure of ENR G93V 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 Residues27
DetailsBINDING SITE FOR RESIDUE NAD A 501
ChainResidue
AGLY13
ASER91
AILE92
AVAL93
ALEU144
ASER145
ALYS163
AALA189
AGLY190
APRO191
AILE192
AALA15
ATCL502
AHOH514
AHOH518
AHOH539
AHOH558
AHOH563
AHOH587
AHOH616
ASER19
AILE20
AGLN40
ALEU44
ACYS63
AASP64
AVAL65

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TCL A 502
ChainResidue
AVAL93
AALA95
ALEU100
ATYR146
ATYR156
APRO191
ALYS205
ANAD501

site_idAC3
Number of Residues28
DetailsBINDING SITE FOR RESIDUE NAD B 503
ChainResidue
BGLY13
BALA15
BSER19
BILE20
BGLN40
BCYS63
BASP64
BVAL65
BSER91
BILE92
BVAL93
BLEU144
BSER145
BTYR146
BLYS163
BALA189
BGLY190
BPRO191
BILE192
BTHR194
BALA196
BALA197
BTCL504
BHOH580
BHOH582
BHOH607
BHOH613
BHOH647

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE TCL B 504
ChainResidue
BVAL93
BALA95
BLEU100
BTYR146
BTYR156
BALA196
BNAD503

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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