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5NDC

Structure of ba3-type cytochrome c oxidase from Thermus thermophilus by serial femtosecond crystallography

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 CU A 601
ChainResidue
AHIS233
AHIS282
AHIS283
AHOH752

site_idAC2
Number of Residues20
Detailsbinding site for residue HEM A 602
ChainResidue
AHIS72
AASN76
ALEU132
ATYR133
APHE385
AHIS386
AVAL389
AALA390
ATHR394
AMET432
AARG449
AARG450
AALA451
AHOH711
AHOH712
AGLY39
AGLN42
AALA43
ATYR46
ATYR65

site_idAC3
Number of Residues24
Detailsbinding site for residue HAS A 603
ChainResidue
ATYR133
ATRP229
AVAL236
ATYR237
AHIS282
ATHR302
ALEU310
AALA313
ALEU353
AGLY360
AGLY363
AASN366
AALA367
AASP372
AHIS376
AHIS384
APHE385
AGLN388
AARG449
AHOH707
AHOH709
AHOH738
AHOH743
AHOH752

site_idAC4
Number of Residues5
Detailsbinding site for residue OLC A 604
ChainResidue
APHE213
ALEU215
ATRP341
ATRP426
AOLC605

site_idAC5
Number of Residues3
Detailsbinding site for residue OLC A 605
ChainResidue
ATRP143
ASER212
AOLC604

site_idAC6
Number of Residues2
Detailsbinding site for residue OLC A 606
ChainResidue
ATRP111
AOLC608

site_idAC7
Number of Residues3
Detailsbinding site for residue OLC A 607
ChainResidue
ATRP167
AARG168
APHE531

site_idAC8
Number of Residues3
Detailsbinding site for residue OLC A 608
ChainResidue
ATRP111
AOLC606
AOLC609

site_idAC9
Number of Residues3
Detailsbinding site for residue OLC A 609
ChainResidue
AASN102
ALEU472
AOLC608

site_idAD1
Number of Residues2
Detailsbinding site for residue OLC A 610
ChainResidue
AARG419
ALEU420

site_idAD2
Number of Residues1
Detailsbinding site for residue OLC A 611
ChainResidue
ATRP341

site_idAD3
Number of Residues1
Detailsbinding site for residue OLC A 612
ChainResidue
BLEU37

site_idAD4
Number of Residues6
Detailsbinding site for residue CUA B 201
ChainResidue
BHIS114
BCYS149
BGLN151
BCYS153
BHIS157
BMET160

site_idAD5
Number of Residues5
Detailsbinding site for residue OLC B 202
ChainResidue
BPHE21
BVAL28
BLEU32
BTYR35
CPHE31

site_idAD6
Number of Residues2
Detailsbinding site for residue OLC C 101
ChainResidue
CALA32
COLC102

site_idAD7
Number of Residues4
Detailsbinding site for residue OLC C 102
ChainResidue
ATRP441
ALEU444
CARG33
COLC101

site_idAD8
Number of Residues4
Detailsbinding site for residue OLC C 103
ChainResidue
BTYR14
BPHE21
BTYR35
CILE12

Functional Information from PROSITE/UniProt
site_idPS00078
Number of Residues49
DetailsCOX2 CO II and nitrous oxide reductase dinuclear copper centers signature. ViHgfhvegtninvevlpgevstvrytfkrpgeyrii......CnqyCglgHqnM
ChainResidueDetails
BVAL112-MET160

site_idPS00077
Number of Residues55
DetailsCOX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WWTGHPiVyfwllpayaiiytilpkqaggklvsdpmarlafllflllstpvgf..HH
ChainResidueDetails
ATRP229-HIS283

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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