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1AR1

Structure at 2.7 Angstrom Resolution of the Paracoccus Denitrificans two-subunit Cytochrome C Oxidase Complexed with an Antibody Fv Fragment

Functional Information from GO Data
ChainGOidnamespacecontents
A0004129molecular_functioncytochrome-c oxidase activity
A0005886cellular_componentplasma membrane
A0006119biological_processoxidative phosphorylation
A0009060biological_processaerobic respiration
A0015990biological_processelectron transport coupled proton transport
A0016020cellular_componentmembrane
A0020037molecular_functionheme binding
A0022904biological_processrespiratory electron transport chain
A0045277cellular_componentrespiratory chain complex IV
A0046872molecular_functionmetal ion binding
A0070469cellular_componentrespirasome
A1902600biological_processproton transmembrane transport
B0004129molecular_functioncytochrome-c oxidase activity
B0005507molecular_functioncopper ion binding
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0022900biological_processelectron transport chain
C0002250biological_processadaptive immune response
C0003823molecular_functionantigen binding
C0016064biological_processimmunoglobulin mediated immune response
C0019814cellular_componentimmunoglobulin complex
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU B 270
ChainResidue
BCYS216
BGLU218
BCYS220
BHIS224
BCU271

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CU B 271
ChainResidue
BHIS181
BCYS216
BCYS220
BMET227
BCU270

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CU A 559
ChainResidue
AHIS276
AHIS325
AHIS326

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 560
ChainResidue
AHIS403
AASP404
AHOH574
BSER217
BGLU218

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 561
ChainResidue
AGLU56
AHIS59
AGLY61
AGLN63
AASP477

site_idAC6
Number of Residues21
DetailsBINDING SITE FOR RESIDUE HEA A 562
ChainResidue
ATHR50
AARG54
ATRP87
AILE91
AHIS94
AMET98
AMET99
AVAL103
AGLY163
ATRP164
ATYR406
AHIS413
AMET416
ASER417
APHE460
AARG473
AARG474
ATYR475
ASER496
APHE503
AHOH575

site_idAC7
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEA A 563
ChainResidue
ATRP164
ATRP272
AVAL279
ATYR280
AHIS325
AHIS326
ATHR344
AILE347
AALA348
ATHR351
AGLY352
AGLY387
AGLY390
ALEU393
ASER394
AASP399
AHIS403
AVAL408
AHIS411
APHE412
AVAL415
AMET416
AARG473
AHOH571
AHOH572

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE LDA B 272
ChainResidue
APHE465
AARG468
ALDA569
BASN19

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE LDA B 273
ChainResidue
BMET18

site_idBC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE LDA A 564
ChainResidue
APHE369

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE LDA A 565
ChainResidue
ATRP363
BASN74
BTRP81

site_idBC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE LDA A 566
ChainResidue
ALEU511
AILE33
ASER436

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE LDA A 568
ChainResidue
ATRP443
AGLY505
AILE506

site_idBC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE LDA B 274
ChainResidue
BVAL90
BALA94
BPRO98

site_idBC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE LDA A 569
ChainResidue
APHE461
BLDA272

site_idCA
Number of Residues4
DetailsNON REDOX ACTIVE CA BINDING SITE.
ChainResidue
AGLU56
AHIS59
AGLY61
AGLN63

site_idCUA
Number of Residues6
DetailsCU A BINDING SITE.
ChainResidue
BHIS181
BCYS216
BGLU218
BCYS220
BHIS224
BMET227

site_idCUB
Number of Residues3
DetailsCU B BINDING SITE.
ChainResidue
AHIS276
AHIS325
AHIS326

site_idHM3
Number of Residues1
DetailsAXIAL HEME A3 LIGAND.
ChainResidue
AHIS411

site_idHMA
Number of Residues2
DetailsAXIAL HEME A LIGANDS.
ChainResidue
AHIS94
AHIS413

site_idMM
Number of Residues3
DetailsNON REDOX ACTIVE MN/MG BINDING SITE.
ChainResidue
AHIS403
AASP404
BGLU218

Functional Information from PROSITE/UniProt
site_idPS00077
Number of Residues55
DetailsCOX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WFFGHPeVyiiilpgfgiishvistfakkpifgylpmvlamaaigilgfvvwa..HH
ChainResidueDetails
ATRP272-HIS326

site_idPS00078
Number of Residues49
DetailsCOX2 CO II and nitrous oxide reductase dinuclear copper centers signature. ViHawtipafavkqdavpgriaqlwfsvdqegvyfgq......CselCginHayM
ChainResidueDetails
BVAL179-MET227

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues170
DetailsTOPO_DOM: Periplasmic
ChainResidueDetails
BGLN1-PRO26
BMET106-ALA251
AMET207-VAL217
ALYS300-PHE303
AGLY365-PHE369
AARG438-TYR440
ALYS515-HIS558

site_idSWS_FT_FI2
Number of Residues62
DetailsTRANSMEM: Helical
ChainResidueDetails
BLEU27-ARG59
BTHR75-GLU105

site_idSWS_FT_FI3
Number of Residues14
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
BPHE60-ASN74
APRO152-GLY176
AGLY252-GLY262
AMET332
AALA396-ASP404
AGLY470-TYR478

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING:
ChainResidueDetails
BHIS181
BCYS216
BGLU218
BCYS220
BHIS224
BMET227

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Pyrrolidone carboxylic acid => ECO:0000269|PubMed:2820725
ChainResidueDetails
BGLN1

site_idSWS_FT_FI6
Number of Residues29
DetailsTRANSMEM: Helical; Name=IV
ChainResidueDetails
ATYR177-ASN206

site_idSWS_FT_FI7
Number of Residues33
DetailsTRANSMEM: Helical; Name=V
ChainResidueDetails
APRO218-PHE251

site_idSWS_FT_FI8
Number of Residues36
DetailsTRANSMEM: Helical; Name=VI
ChainResidueDetails
AASP263-LYS299

site_idSWS_FT_FI9
Number of Residues27
DetailsTRANSMEM: Helical; Name=VII
ChainResidueDetails
AGLY304-GLY331

site_idSWS_FT_FI10
Number of Residues31
DetailsTRANSMEM: Helical; Name=VIII
ChainResidueDetails
ASER333-GLY364

site_idSWS_FT_FI11
Number of Residues25
DetailsTRANSMEM: Helical; Name=IX
ChainResidueDetails
ALYS370-GLN395

site_idSWS_FT_FI12
Number of Residues32
DetailsTRANSMEM: Helical; Name=X
ChainResidueDetails
ATHR405-GLY437

site_idSWS_FT_FI13
Number of Residues28
DetailsTRANSMEM: Helical; Name=XI
ChainResidueDetails
APRO441-GLN469

site_idSWS_FT_FI14
Number of Residues35
DetailsTRANSMEM: Helical; Name=XII
ChainResidueDetails
APRO479-GLY514

site_idSWS_FT_FI15
Number of Residues3
DetailsBINDING: axial binding residue
ChainResidueDetails
AHIS94
AHIS411
AHIS413

site_idSWS_FT_FI16
Number of Residues4
DetailsBINDING:
ChainResidueDetails
AHIS276
ATYR280
AHIS325
AHIS326

site_idSWS_FT_FI17
Number of Residues2
DetailsCROSSLNK: 1'-histidyl-3'-tyrosine (His-Tyr)
ChainResidueDetails
AHIS276
ATYR280

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 9788998
ChainResidueDetails
AGLU278
ALYS354

223532

PDB entries from 2024-08-07

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