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1I2Z

E. COLI ENOYL REDUCTASE IN COMPLEX WITH NAD AND BRL-12654

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 Residues22
DetailsBINDING SITE FOR RESIDUE NAD A 501
ChainResidue
AGLY13
AILE92
AGLY93
ALEU144
ASER145
ATYR146
ALYS163
AALA189
AGLY190
APRO191
AILE192
AALA15
ATHR194
ALEU195
AHOH2061
ASER19
AILE20
AGLN40
ACYS63
AASP64
AVAL65
ASER91

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE 654 A 502
ChainResidue
ATYR146
AALA196
APHE203

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE NAD B 1501
ChainResidue
BGLY1013
BALA1015
BSER1019
BILE1020
BGLN1040
BCYS1063
BASP1064
BVAL1065
BSER1091
BILE1092
BLEU1144
BSER1145
BLYS1163
BALA1189
BGLY1190
BPRO1191
BILE1192
BTHR1194
BLEU1195
B6541502
BHOH2060

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE 654 B 1502
ChainResidue
BPHE1203
BNAD1501

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
ALEU147
AASN157
BLEU1147
BASN1157

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
AVAL14
BASN1041
BVAL1065
BGLY1093
BALA1164
BARG1193
AILE20
AASN41
AVAL65
AGLY93
AALA164
AARG193
BVAL1014
BILE1020

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
APRO96
BPRO1096

site_idSWS_FT_FI4
Number of Residues6
DetailsSITE: Involved in acyl-ACP binding
ChainResidueDetails
AASP202
ALYS205
AMET206
BASP1202
BLYS1205
BMET1206

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qsg
ChainResidueDetails
AGLU150

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qsg
ChainResidueDetails
BGLU1150

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1qsg
ChainResidueDetails
ATYR156
ALYS163

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1qsg
ChainResidueDetails
BLYS1163
BTYR1156

site_idCSA5
Number of Residues2
DetailsAnnotated By Reference To The Literature 1qsg
ChainResidueDetails
AMET159
ALYS163

site_idCSA6
Number of Residues2
DetailsAnnotated By Reference To The Literature 1qsg
ChainResidueDetails
BLYS1163
BMET1159

site_idMCSA1
Number of Residues2
DetailsM-CSA 606
ChainResidueDetails
AASN157proton acceptor, proton donor
AALA164electrostatic stabiliser

site_idMCSA2
Number of Residues2
DetailsM-CSA 606
ChainResidueDetails
BASN1157proton acceptor, proton donor
BALA1164electrostatic stabiliser

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PDB entries from 2024-07-10

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