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

8D4T

Mammalian CIV with GDN bound

Functional Information from GO Data
ChainGOidnamespacecontents
M0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
M0045277cellular_componentrespiratory chain complex IV
N0004129molecular_functioncytochrome-c oxidase activity
N0005739cellular_componentmitochondrion
N0005743cellular_componentmitochondrial inner membrane
N0006119biological_processoxidative phosphorylation
N0009060biological_processaerobic respiration
N0016020cellular_componentmembrane
N0020037molecular_functionheme binding
N0022904biological_processrespiratory electron transport chain
N0045277cellular_componentrespiratory chain complex IV
N0046872molecular_functionmetal ion binding
N1902600biological_processproton transmembrane transport
O0004129molecular_functioncytochrome-c oxidase activity
O0005507molecular_functioncopper ion binding
O0005739cellular_componentmitochondrion
O0005743cellular_componentmitochondrial inner membrane
O0016020cellular_componentmembrane
O0016491molecular_functionoxidoreductase activity
O0022900biological_processelectron transport chain
O0031966cellular_componentmitochondrial membrane
O0042773biological_processATP synthesis coupled electron transport
O0045277cellular_componentrespiratory chain complex IV
O0046872molecular_functionmetal ion binding
O1902600biological_processproton transmembrane transport
P0004129molecular_functioncytochrome-c oxidase activity
P0005739cellular_componentmitochondrion
P0005743cellular_componentmitochondrial inner membrane
P0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
P0008535biological_processrespiratory chain complex IV assembly
P0009055molecular_functionelectron transfer activity
P0016020cellular_componentmembrane
P0019646biological_processaerobic electron transport chain
P0022904biological_processrespiratory electron transport chain
P0045277cellular_componentrespiratory chain complex IV
P1902600biological_processproton transmembrane transport
Q0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
Q0045277cellular_componentrespiratory chain complex IV
R0005743cellular_componentmitochondrial inner membrane
R0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
R0045277cellular_componentrespiratory chain complex IV
S0005740cellular_componentmitochondrial envelope
S0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
S0045277cellular_componentrespiratory chain complex IV
T0005743cellular_componentmitochondrial inner membrane
U0005739cellular_componentmitochondrion
U0005743cellular_componentmitochondrial inner membrane
U0006119biological_processoxidative phosphorylation
U0016020cellular_componentmembrane
U0045277cellular_componentrespiratory chain complex IV
V0005739cellular_componentmitochondrion
V0005743cellular_componentmitochondrial inner membrane
V0006119biological_processoxidative phosphorylation
V0016020cellular_componentmembrane
V0045277cellular_componentrespiratory chain complex IV
W0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
W0045277cellular_componentrespiratory chain complex IV
X0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
Y0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
Y0045277cellular_componentrespiratory chain complex IV
Functional Information from PROSITE/UniProt
site_idPS00077
Number of Residues56
DetailsCOX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WFFGHPeVyililpgfgmishivtyysgkkepfgymgmvwammsigflgfivwa.HH
ChainResidueDetails
NTRP236-HIS291

site_idPS00078
Number of Residues49
DetailsCOX2 CO II and nitrous oxide reductase dinuclear copper centers signature. VlHswavpslglktdaipgrlnqttlmssrpglyygq......CseiCgsnHsfM
ChainResidueDetails
OVAL159-MET207

site_idPS00848
Number of Residues23
DetailsCOX5B_1 Cytochrome c oxidase subunit Vb, zinc binding region signature. VIWfwlhkgeaqrCpsCGthYKL
ChainResidueDetails
SVAL69-LEU91

site_idPS01329
Number of Residues18
DetailsCOX6A Cytochrome c oxidase subunit VIa signature. IRtKpFsWGDGnHTfFhN
ChainResidueDetails
TILE55-ASN72

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsTOPO_DOM: Mitochondrial matrix => ECO:0000269|PubMed:30030519
ChainResidueDetails
MILE26-GLY36
SCYS62
SCYS82
SCYS85
NSER401-ASN406

site_idSWS_FT_FI2
Number of Residues23
DetailsTRANSMEM: Helical => ECO:0000250|UniProtKB:P10175
ChainResidueDetails
MILE37-SER60
SLYS55
SLYS90
PTYR257-SER261

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17665
ChainResidueDetails
YLYS9
QSER36

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P19783
ChainResidueDetails
QLYS38
PGLU153-ASP155
PLYS224-HIS232

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P19783
ChainResidueDetails
QLYS45
OCYS196
OGLU198
OCYS200
OHIS204
OMET207

site_idSWS_FT_FI6
Number of Residues23
DetailsTRANSMEM: Helical; Name=IV => ECO:0000269|PubMed:27605664
ChainResidueDetails
PVAL129-MET152
NARG213-ASP227
NVAL287-ASP298

site_idSWS_FT_FI7
Number of Residues27
DetailsTRANSMEM: Helical; Name=V => ECO:0000269|PubMed:27605664
ChainResidueDetails
PARG156-GLU183

site_idSWS_FT_FI8
Number of Residues32
DetailsTRANSMEM: Helical; Name=VI => ECO:0000269|PubMed:27605664
ChainResidueDetails
PGLY191-LEU223

site_idSWS_FT_FI9
Number of Residues23
DetailsTRANSMEM: Helical; Name=VII => ECO:0000269|PubMed:27605664
ChainResidueDetails
PPHE233-ILE256

site_idSWS_FT_FI10
Number of Residues16
DetailsTRANSMEM: Helical; Name=VII => ECO:0000269|PubMed:27605664
ChainResidueDetails
NTYR270-ILE286

site_idSWS_FT_FI11
Number of Residues28
DetailsTRANSMEM: Helical; Name=VIII => ECO:0000269|PubMed:27605664
ChainResidueDetails
NVAL299-LEU327

site_idSWS_FT_FI12
Number of Residues7
DetailsTOPO_DOM: Mitochondrial matrix => ECO:0000269|PubMed:27605664
ChainResidueDetails
NHIS328-SER335

site_idSWS_FT_FI13
Number of Residues21
DetailsTRANSMEM: Helical; Name=IX => ECO:0000269|PubMed:27605664
ChainResidueDetails
NPRO336-VAL357

site_idSWS_FT_FI14
Number of Residues24
DetailsTOPO_DOM: Mitochondrial intermembrane => ECO:0000269|PubMed:27605664
ChainResidueDetails
NLEU358-THR370
NSER434-ALA446

site_idSWS_FT_FI15
Number of Residues29
DetailsTRANSMEM: Helical; Name=X => ECO:0000269|PubMed:27605664
ChainResidueDetails
NTYR371-PHE400

site_idSWS_FT_FI16
Number of Residues26
DetailsTRANSMEM: Helical; Name=XI => ECO:0000269|PubMed:27605664
ChainResidueDetails
NASP407-LEU433

site_idSWS_FT_FI17
Number of Residues31
DetailsTRANSMEM: Helical; Name=XII => ECO:0000269|PubMed:27605664
ChainResidueDetails
NTYR447-SER478

site_idSWS_FT_FI18
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:27605664, ECO:0000305|PubMed:23537388
ChainResidueDetails
NGLU40
NGLY45
NSER441

site_idSWS_FT_FI19
Number of Residues3
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:20385840, ECO:0000269|PubMed:8638158
ChainResidueDetails
NHIS61
NHIS376
NHIS378

site_idSWS_FT_FI20
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:20385840, ECO:0000269|PubMed:8638158
ChainResidueDetails
NHIS240
NHIS290
NHIS291
NHIS368
NASP369

site_idSWS_FT_FI21
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
NTYR244

site_idSWS_FT_FI22
Number of Residues1
DetailsMOD_RES: N-formylmethionine => ECO:0000269|PubMed:2165784
ChainResidueDetails
NFME1

site_idSWS_FT_FI23
Number of Residues2
DetailsCROSSLNK: 1'-histidyl-3'-tyrosine (His-Tyr) => ECO:0000269|PubMed:10338009
ChainResidueDetails
NHIS240
NTYR244

Catalytic Information from CSA
site_idMCSA1
Number of Residues14
DetailsM-CSA 124
ChainResidueDetails

237735

PDB entries from 2025-06-18

PDB statisticsPDBj update infoContact PDBjnumon