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4FAA

Structure of Recombinant Cytochrome ba3 Oxidase mutant A120F+A204F from Thermus thermophilus

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 Residues4
DetailsBINDING SITE FOR RESIDUE CU A 601
ChainResidue
AHIS233
AHIS282
AHIS283
APEO604

site_idAC2
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM A 602
ChainResidue
ATYR65
AHIS72
AASN76
AALA77
ALEU132
ATYR133
APHE385
AHIS386
AVAL389
AALA390
ATHR394
AMET432
AMET435
AARG449
AARG450
AALA451
ALEU477
AHOH715
ALEU32
AGLY39
AGLN42
AALA43
ATYR46

site_idAC3
Number of Residues30
DetailsBINDING SITE FOR RESIDUE HAS A 603
ChainResidue
ATYR133
ATRP229
AVAL236
ATYR237
ATRP239
AHIS282
AHIS283
ASER309
AALA313
AALA317
ALEU353
APHE356
AILE357
AGLY360
AGLY363
AILE364
AASN366
AALA367
AASP372
AHIS376
AVAL381
AHIS384
APHE385
AGLN388
AVAL389
AARG449
APEO604
AHOH701
AHOH719
AHOH749

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEO A 604
ChainResidue
AHIS233
AVAL236
AHIS283
ACU601
AHAS603

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE OLC A 605
ChainResidue
APRO358
AHIS440
ALEU444
BOLC203
CGLY25
CVAL29
COLC101

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OLC A 606
ChainResidue
AVAL158
ATYR161
AILE475
AVAL476
AOLC614
AOLC615

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OLC A 607
ChainResidue
APHE213
ALEU215
ATRP341
ATRP426
AOLC614
AOLC615

site_idAC8
Number of Residues3
DetailsBINDING SITE FOR RESIDUE OLC A 608
ChainResidue
APRO292
AVAL300
BHOH304

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OLC A 609
ChainResidue
ALYS140
ASER212
APHE213
ALEU430
AOLC616
AHOH703

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE OLC A 610
ChainResidue
ATRP111
AOLC613

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OLC A 611
ChainResidue
ATYR161
ALEU164
AARG168
AOLC612

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE OLC A 612
ChainResidue
AGLY528
AOLC611
ATRP167
AARG168
ALYS171

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OLC A 613
ChainResidue
AGLY104
ATRP111
AOLC610
AOLC614

site_idBC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE OLC A 614
ChainResidue
AASN102
ALEU108
ASER150
AVAL151
ALEU154
AVAL471
ALEU472
AOLC606
AOLC607
AOLC613
AOLC615
AHOH736

site_idBC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE OLC A 615
ChainResidue
AVAL205
AASP415
AALA416
AARG419
AOLC606
AOLC607
AOLC614

site_idBC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE OLC A 616
ChainResidue
AARG337
ATRP341
ATRP426
ALEU430
AILE434
AOLC609
AHOH745

site_idBC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CUA B 201
ChainResidue
BHIS114
BCYS149
BGLN151
BCYS153
BHIS157
BMET160

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OLC B 202
ChainResidue
BPHE21
BVAL28
BLEU32
BTYR35
BOLC204
CPHE31

site_idCC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE OLC B 203
ChainResidue
ATRP441
AOLC605
BGLY120
BARG141
BGLU144
BHOH331
CVAL29
CARG33
COLC101

site_idCC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE OLC B 204
ChainResidue
BALA13
BTYR14
BPHE21
BTYR35
BOLC202
CLEU9
CILE12

site_idCC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE OLC C 101
ChainResidue
AOLC605
BOLC203
CTHR18

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 2024-10-16

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