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3QJS

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
A0070469cellular_componentrespirasome
A1902600biological_processproton transmembrane transport
B0004129molecular_functioncytochrome-c oxidase activity
B0005507molecular_functioncopper ion binding
B0005886cellular_componentplasma membrane
B0016020cellular_componentmembrane
B0046872molecular_functionmetal ion binding
B0070469cellular_componentrespirasome
B1902600biological_processproton transmembrane transport
C0004129molecular_functioncytochrome-c oxidase activity
C0005886cellular_componentplasma membrane
C0006811biological_processmonoatomic ion transport
C0016020cellular_componentmembrane
C0070469cellular_componentrespirasome
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 Residues26
DetailsBINDING SITE FOR RESIDUE HEM A 800
ChainResidue
AALA43
ATYR46
ATYR65
ALEU69
AHIS72
AASN76
AALA77
ALEU132
ATYR133
APHE385
AHIS386
AALA390
ATHR394
ATRP428
AMET435
AARG449
AARG450
AALA451
ALEU477
AHOH564
AHOH574
ALEU32
ASER36
AGLY39
APRO40
AGLN42

site_idAC3
Number of Residues29
DetailsBINDING SITE FOR RESIDUE HAS A 801
ChainResidue
ATYR133
ATRP229
AVAL236
ATYR237
ATRP239
AHIS282
AHIS283
AALA306
ASER309
ALEU310
AALA313
ALEU353
ALEU354
APHE356
AGLY360
AGLY363
AASN366
AALA367
AASP372
AHIS376
AVAL381
AHIS384
APHE385
AGLN388
AVAL389
AARG449
ACMO563
AHOH565
AHOH576

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

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CMO A 563
ChainResidue
AHIS233
AHIS283
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 Residues30
DetailsTRANSMEM: Helical
ChainResidueDetails
CLYS4-GLY34
APHE385-LEU405
ALEU420-HIS440
AVAL471-VAL491
AILE527-VAL547
AVAL74-ALA94
ALEU105-LEU125
AALA144-LEU164
AVAL187-PHE207
ALEU227-ILE247
ALEU267-ASP287
AVAL300-LEU320
AALA345-VAL365

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-formylmethionine => ECO:0000269|PubMed:11152118
ChainResidueDetails
CMET1
AHIS384
AHIS386

site_idSWS_FT_FI3
Number of Residues129
DetailsTOPO_DOM: Periplasmic
ChainResidueDetails
BTHR39-GLU168
ATYR237

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING:
ChainResidueDetails
BHIS114
BCYS149
BCYS153
BHIS157

site_idSWS_FT_FI5
Number of Residues2
DetailsCROSSLNK: 1'-histidyl-3'-tyrosine (His-Tyr)
ChainResidueDetails
AHIS233
ATYR237

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

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PDB entries from 2024-04-24

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