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3S8F

1.8 A structure of ba3 cytochrome c oxidase from Thermus thermophilus in lipid environment

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
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
C0070469cellular_componentrespirasome
C1902600biological_processproton transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CU A 803
ChainResidue
AHIS233
AHIS282
AHIS283
APER563

site_idAC2
Number of Residues26
DetailsBINDING SITE FOR RESIDUE HEM A 800
ChainResidue
ATYR46
ATYR65
ALEU69
AHIS72
AASN76
AALA77
ALEU132
ATYR133
APHE385
AHIS386
AALA390
ATHR394
AMET432
AMET435
AARG449
AARG450
AALA451
ALEU477
AHOH608
AHOH616
AHOH619
ALEU32
AGLY39
APRO40
AGLN42
AALA43

site_idAC3
Number of Residues28
DetailsBINDING SITE FOR RESIDUE HAS A 801
ChainResidue
ATYR133
ATRP229
AVAL236
ATYR237
AHIS282
AHIS283
ATHR302
ASER309
ALEU310
AALA313
ALEU353
APHE356
AGLY360
AGLY363
AASN366
AALA367
AASP372
AHIS376
AVAL381
AHIS384
APHE385
AGLN388
AARG449
APER563
AHOH621
AHOH684
AHOH685
AHOH689

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PER A 563
ChainResidue
AHIS233
AVAL236
AHIS283
AHAS801
ACU803

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE OLC A 564
ChainResidue
APRO358
AMET433
AHIS440
BOLC170
CPHE22
CGLY25
CALA32
COLC35

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OLC A 565
ChainResidue
ATYR161
AILE475
AOLC572
AOLC573

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE OLC A 566
ChainResidue
AILE115
APHE213
ALEU215
ATRP341
ATRP426
AOLC567
AOLC571
AOLC572
AOLC573

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE OLC A 567
ChainResidue
ATRP143
ASER212
APHE213
AGLY214
AOLC566
AOLC574
AHOH578

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE OLC A 568
ChainResidue
ATRP111
AOLC571

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE OLC A 569
ChainResidue
ATYR161
ALEU164
AASP165
AARG168
AOLC570

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE OLC A 570
ChainResidue
AARG168
ALYS171
AGLY528
AOLC569
ATRP167

site_idBC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE OLC A 571
ChainResidue
AGLY104
ALEU108
ATRP111
AVAL465
AVAL468
AOLC566
AOLC568
AOLC572
AOLC574

site_idBC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE OLC A 572
ChainResidue
AASN102
AGLY104
ALEU108
AMET112
AVAL151
AOLC565
AOLC566
AOLC571
AOLC573
AHOH585

site_idBC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE OLC A 573
ChainResidue
AASP415
AALA416
AARG419
AOLC565
AOLC566
AOLC572
AHOH575
AHOH690

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OLC A 574
ChainResidue
AARG337
ATRP341
ATRP426
AOLC567
AOLC571
AHOH680

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CUA B 802
ChainResidue
BHIS114
BCYS149
BGLN151
BCYS153
BHIS157
BMET160

site_idBC8
Number of Residues8
DetailsBINDING SITE FOR RESIDUE OLC B 169
ChainResidue
BPHE21
BVAL28
BVAL28
BLEU32
BTYR35
BOLC171
BHOH185
CPHE31

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OLC B 170
ChainResidue
AOLC564
AHOH583
BGLY120
BARG141
BGLU144
CARG33

site_idCC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OLC B 171
ChainResidue
BALA13
BTYR14
BGLY17
BPHE21
BTYR35
BOLC169

site_idCC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OLC B 172
ChainResidue
APRO292
AILE297
BALA42
BHOH182

site_idCC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OLC C 35
ChainResidue
AOLC564
CVAL14
CTHR18
CVAL21

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 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 2024-07-31

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