Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3S3A

Structure of Thermus thermophilus cytochrome ba3 oxidase 120s after Xe depressurization

Functional Information from GO Data
ChainGOidnamespacecontents
A0004129molecular_functioncytochrome-c oxidase activity
A0005886cellular_componentplasma membrane
A0006119biological_processoxidative phosphorylation
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
C1902600biological_processproton transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU A 803
ChainResidue
AHIS233
AHIS282
AHIS283

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE HEM A 800
ChainResidue
AHIS72
AASN76
AALA77
ALEU132
ATYR133
APHE385
AHIS386
AVAL389
ATHR394
AARG449
AARG450
AALA451
ASER36
AGLY39
AGLN42
ATYR46
ATYR65
ALEU69

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HAS A 801
ChainResidue
ATYR133
ATRP229
AVAL236
ATYR237
ATRP239
AHIS282
ASER309
AALA313
ATRP335
AVAL350
ALEU353
ALEU354
APHE356
AGLY360
AASN366
AALA367
AASP372
AHIS376
AVAL381
AHIS384
APHE385
AGLN388
AVAL389
AARG449

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

site_idAC5
Number of Residues1
DetailsBINDING SITE FOR RESIDUE XE A 563
ChainResidue
AGLY232

Functional Information from PROSITE/UniProt
site_idPS00077
Number of Residues55
DetailsCOX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WWTGHPiVyfwllpayaiiytilpkqaggklvsdpmarlafllflllstpvgf..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 Residues129
DetailsTOPO_DOM: Periplasmic
ChainResidueDetails
BTHR39-GLU168
AHIS384
AHIS386

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING:
ChainResidueDetails
BHIS114
BCYS149
BCYS153
BHIS157

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AHIS282
AHIS283

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

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon