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2RG1

Crystal structure of E. coli WrbA apoprotein

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 Residues5
DetailsBINDING SITE FOR RESIDUE CL A 200
ChainResidue
ASER9
AMET10
ATYR11
AHIS13
AILE14

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 200
ChainResidue
BILE14
BSER9
BMET10
BTYR11
BHIS13

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
ASER9
ATHR77
ASER112
AHIS132
BSER9
BTHR77
BSER112
BHIS132

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:17951395
ChainResidueDetails
ATYR11
AALA50
AASP168
BTYR11
BALA50
BASP168

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01017, ECO:0000305|PubMed:17951395
ChainResidueDetails
ATRP97
BTRP97

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS49
BLYS49

222415

PDB entries from 2024-07-10

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