Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4N4Y

Structure of Recombinant Cytochrome ba3 Oxidase mutant G232V 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 Residues24
DetailsBINDING SITE FOR RESIDUE HEM A 602
ChainResidue
ATYR65
ALEU69
AHIS72
AASN76
ALEU132
ATYR133
APHE385
AHIS386
AALA390
ATHR394
AMET432
AMET435
AARG449
AARG450
AALA451
ALEU477
AHOH736
AHOH744
AHOH747
ALEU32
AGLY39
AGLN42
AALA43
ATYR46

site_idAC3
Number of Residues28
DetailsBINDING SITE FOR RESIDUE HAS A 603
ChainResidue
ATYR133
ATRP229
AVAL236
ATYR237
AHIS282
AHIS283
ASER309
ALEU310
AALA313
AALA317
AVAL350
ALEU353
ALEU354
APHE356
AGLY360
AGLY363
AASN366
AALA367
AASP372
AHIS376
AHIS384
APHE385
AGLN388
AARG449
APEO604
AHOH701
AHOH812
AHOH813

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE PEO A 604
ChainResidue
AHIS233
AVAL236
AHIS283
ACU601
AHAS603
AHOH734

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OLC A 605
ChainResidue
ALEU105
AVAL158
ATYR161
AILE475
AOLC613
AOLC614

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE OLC A 606
ChainResidue
AILE115
APHE213
ALEU215
ATRP341
AVAL347
ATRP426
AOLC612
AOLC613
AOLC614

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OLC A 607
ChainResidue
ATHR293
AILE297
APHE304
AHOH712

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE OLC A 608
ChainResidue
ATRP143
ASER212
ALEU430
AOLC615
AHOH707

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE OLC A 609
ChainResidue
ATRP111
AOLC612

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OLC A 610
ChainResidue
ATYR161
ALEU164
AARG168
AOLC611

site_idBC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OLC A 611
ChainResidue
ATRP167
AARG168
AGLY528
AOLC610

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OLC A 612
ChainResidue
AOLC606
AOLC609
AOLC613
AGLY104
ALEU108
APHE469

site_idBC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE OLC A 613
ChainResidue
AASN102
ALEU105
ALEU108
AMET112
ALEU209
ALEU472
AOLC605
AOLC606
AOLC612
AOLC614
AHOH715

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OLC A 614
ChainResidue
AARG419
AOLC605
AOLC606
AOLC613
AHOH702
AHOH704

site_idBC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OLC A 615
ChainResidue
AARG337
ATRP341
AOLC608
AHOH808

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CUA B 201
ChainResidue
BHIS114
BCYS149
BGLN151
BCYS153
BHIS157
BMET160

site_idBC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OLC B 202
ChainResidue
BPHE21
BLEU32
BTYR35
BOLC204
BHOH306
CPHE31

site_idBC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE OLC B 203
ChainResidue
ATRP441
AHOH713
AHOH714
BARG141
BGLU144
BTYR145
COLC101
COLC102

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE OLC B 204
ChainResidue
BALA13
BGLY17
BPHE21
BOLC202

site_idCC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE OLC C 101
ChainResidue
APRO358
AHIS440
BOLC203
CPHE22
CGLY25
CVAL29
COLC102

site_idCC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE OLC C 102
ChainResidue
BOLC203
CTHR18
COLC101

Functional Information from PROSITE/UniProt
site_idPS00077
Number of Residues55
DetailsCOX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WWTVHPiVyfwllpayaiiytilpkqaggklvsdpmarlafllflllstpvgf..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

227344

PDB entries from 2024-11-13

PDB statisticsPDBj update infoContact PDBjnumon