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3B6K

WrbA from Escherichia coli, Benzoquinone complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
A0005829cellular_componentcytosol
A0006979biological_processresponse to oxidative stress
A0008753molecular_functionNADPH dehydrogenase (quinone) activity
A0010181molecular_functionFMN binding
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0032991cellular_componentprotein-containing complex
A0042802molecular_functionidentical protein binding
A0050136molecular_functionNADH:ubiquinone reductase (non-electrogenic) activity
A0050660molecular_functionflavin adenine dinucleotide binding
A0050661molecular_functionNADP binding
A0051287molecular_functionNAD binding
B0000166molecular_functionnucleotide binding
B0003955molecular_functionNAD(P)H dehydrogenase (quinone) activity
B0005829cellular_componentcytosol
B0006979biological_processresponse to oxidative stress
B0008753molecular_functionNADPH dehydrogenase (quinone) activity
B0010181molecular_functionFMN binding
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0032991cellular_componentprotein-containing complex
B0042802molecular_functionidentical protein binding
B0050136molecular_functionNADH:ubiquinone reductase (non-electrogenic) activity
B0050660molecular_functionflavin adenine dinucleotide binding
B0050661molecular_functionNADP binding
B0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FMN A 200
ChainResidue
ASER10
APHE80
ASER113
ATHR114
AGLY115
ATHR116
AGLY117
AGLY118
APLQ201
AHOH251
AHOH252
AMET11
AHOH253
AHOH379
BASP92
BHIS133
ATYR12
AGLY13
AHIS14
AILE15
APRO77
ATHR78
AARG79

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FMN B 200
ChainResidue
AASP92
AHIS133
BSER10
BMET11
BTYR12
BGLY13
BHIS14
BILE15
BPRO77
BTHR78
BARG79
BPHE80
BSER113
BTHR114
BGLY115
BTHR116
BGLY117
BGLY118
BPLQ201
BHOH271
BHOH272
BHOH273
BHOH399

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PLQ A 201
ChainResidue
AFMN200
AHOH384
AHOH385
AHOH388
AHOH389
BGLY95
BTRP98

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PLQ B 201
ChainResidue
ATRP98
BFMN200
BHOH403
BHOH408
BHOH410

site_idAC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 15P B 202
ChainResidue
ATYR143
AALA144
APHE149
BTRP98
BALA99
BSER100
BGLY101
BHOH263
BHOH359

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE 15P A 202
ChainResidue
ATRP98
AALA99
ASER100
AGLY101
AHOH370
BTYR143
BALA144
BGLN146
BHOH364

site_idAC7
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 15P B 203
ChainResidue
AGLU49
ALYS50
AGLY52
AGLY53
AGLY105
ALEU196
AASN197
AHOH327
BTYR188
BLEU192
BLYS195

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 15P A 203
ChainResidue
ATYR188
ALEU192
ALYS195
AHOH322
AHOH395
BASN197

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01017, ECO:0000269|PubMed:17951395, ECO:0000269|PubMed:19665595
ChainResidueDetails
ASER10
ATHR78
ASER113
AHIS133
BSER10
BTHR78
BSER113
BHIS133

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:17951395
ChainResidueDetails
ATYR12
AALA51
AASP169
BTYR12
BALA51
BASP169

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01017, ECO:0000305|PubMed:17951395
ChainResidueDetails
ATRP98
BTRP98

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS50
BLYS50

218853

PDB entries from 2024-04-24

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