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3E9J

Structure of the charge-transfer intermediate of the transmembrane redox catalyst DsbB

Functional Information from GO Data
ChainGOidnamespacecontents
B0003756molecular_functionprotein disulfide isomerase activity
B0005515molecular_functionprotein binding
B0015035molecular_functionprotein-disulfide reductase activity
B0015036molecular_functiondisulfide oxidoreductase activity
B0016491molecular_functionoxidoreductase activity
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042597cellular_componentperiplasmic space
B0071236biological_processcellular response to antibiotic
C0005515molecular_functionprotein binding
C0005886cellular_componentplasma membrane
C0006457biological_processprotein folding
C0009055molecular_functionelectron transfer activity
C0009408biological_processresponse to heat
C0015035molecular_functionprotein-disulfide reductase activity
C0016020cellular_componentmembrane
C0016491molecular_functionoxidoreductase activity
C0016672molecular_functionoxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor
C0048039molecular_functionubiquinone binding
E0003756molecular_functionprotein disulfide isomerase activity
E0005515molecular_functionprotein binding
E0015035molecular_functionprotein-disulfide reductase activity
E0015036molecular_functiondisulfide oxidoreductase activity
E0016491molecular_functionoxidoreductase activity
E0030288cellular_componentouter membrane-bounded periplasmic space
E0042597cellular_componentperiplasmic space
E0071236biological_processcellular response to antibiotic
F0005515molecular_functionprotein binding
F0005886cellular_componentplasma membrane
F0006457biological_processprotein folding
F0009055molecular_functionelectron transfer activity
F0009408biological_processresponse to heat
F0015035molecular_functionprotein-disulfide reductase activity
F0016020cellular_componentmembrane
F0016491molecular_functionoxidoreductase activity
F0016672molecular_functionoxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor
F0048039molecular_functionubiquinone binding
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE UQ1 C 501
ChainResidue
CLYS39
CCYS41
CCYS44
CGLU47
CARG48
CHIS91
CMET142
CLEU146

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE UQ1 F 501
ChainResidue
FPRO40
FCYS41
FCYS44
FGLU47
FARG48
FHIS91
FMET142
FLEU146
FLYS39

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues260
DetailsDomain: {"description":"Thioredoxin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00691","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues96
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues34
DetailsTopological domain: {"description":"Periplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 734
ChainResidueDetails
BHIS41electrofuge, electrophile, nucleofuge, nucleophile
BASP44electrofuge, electrophile, nucleofuge, nucleophile
BLYS48electrostatic stabiliser
BSER104covalently attached, nucleofuge, nucleophile

site_idMCSA2
Number of Residues4
DetailsM-CSA 734
ChainResidueDetails

238895

PDB entries from 2025-07-16

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