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3QJT

The structure of and photolytic induced changes of carbon monoxide binding to the cytochrome ba3-oxidase from Thermus thermophilus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004129molecular_functioncytochrome-c oxidase activity
A0005886cellular_componentplasma membrane
A0006119biological_processoxidative phosphorylation
A0006811biological_processmonoatomic ion transport
A0009060biological_processaerobic respiration
A0016020cellular_componentmembrane
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
A1902600biological_processproton transmembrane transport
B0004129molecular_functioncytochrome-c oxidase activity
B0005507molecular_functioncopper ion binding
B0005886cellular_componentplasma membrane
B0016020cellular_componentmembrane
B0046872molecular_functionmetal ion binding
B1902600biological_processproton transmembrane transport
C0004129molecular_functioncytochrome-c oxidase activity
C0005886cellular_componentplasma membrane
C0006811biological_processmonoatomic ion transport
C0016020cellular_componentmembrane
C1902600biological_processproton transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU1 A 803
ChainResidue
AHIS233
AHIS282
AHIS283
ACMO563

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM A 800
ChainResidue
ATYR65
ALEU69
AHIS72
AASN76
AALA77
ATYR133
APHE385
AHIS386
AVAL389
AALA390
ATHR394
ATRP428
AMET432
AMET435
AARG449
AARG450
AALA451
ALEU477
ASER36
AGLY39
APRO40
AGLN42
ATYR46

site_idAC3
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HAS A 801
ChainResidue
ATYR133
AVAL236
ATYR237
ATRP239
AHIS282
ATHR302
ASER309
ALEU310
AALA313
ALEU320
AVAL350
ALEU353
APHE356
AGLY363
AASN366
AALA367
AASP372
AHIS376
AVAL381
AHIS384
APHE385
AGLN388
AVAL389
AARG449
ACMO563

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CUA B 802
ChainResidue
BHIS114
BCYS149
BGLN151
BCYS153
BHIS157
BMET160

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CMO A 563
ChainResidue
AHIS233
AHIS283
AHIS384
AHAS801
ACU1803

Functional Information from PROSITE/UniProt
site_idPS00077
Number of Residues55
DetailsCOX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WWTGHPiVyfwllpayaiiytilpkqaggrlvsdpmarlafllflllstpvgf..HH
ChainResidueDetails
ATRP229-HIS283

site_idPS00078
Number of Residues49
DetailsCOX2 CO II and nitrous oxide reductase dinuclear copper centers signature. ViHgfhvegtninvevlpgevstvrytfkrpgeyrii......CnqyCglgHqnM
ChainResidueDetails
BVAL112-MET160

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues260
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsCross-link: {"description":"1'-histidyl-3'-tyrosine (His-Tyr)"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues64
DetailsTransmembrane: {"description":"Helical"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues129
DetailsTopological domain: {"description":"Periplasmic"}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 735
ChainResidueDetails
BPHE86electron shuttle
BPHE88electron shuttle
AHIS384electron shuttle
APHE385electron shuttle
AHIS386electron shuttle
AARG449electron shuttle
AARG450electron shuttle

238895

PDB entries from 2025-07-16

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