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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9CE2

Respiratory supercomplex I+III2+IV open state

This is a non-PDB format compatible entry.
Functional Information from PROSITE/UniProt
site_idPS00012
Number of Residues16
DetailsPHOSPHOPANTETHEINE Phosphopantetheine attachment site. DLGLDSLDQVEIIMAM
ChainResidueDetails
OASP107-MET122
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DIDAEKLMCpqEI
ChainResidueDetails
OASP132-ILE144
site_idPS00077
Number of Residues56
DetailsCOX1_CUB Heme-copper oxidase catalytic subunit, copper B binding region signature. WFFGHPeVyililpgfgmishivtyysgkkepfgymgmvwammsigflgfivwa.HH
ChainResidueDetails
AkTRP236-HIS291
site_idPS00078
Number of Residues49
DetailsCOX2 CO II and nitrous oxide reductase dinuclear copper centers signature. VlHswavpslglktdaipgrlnqttlmstrpglyygq......CseiCgsnHsfM
ChainResidueDetails
AlVAL159-MET207
site_idPS00143
Number of Residues24
DetailsINSULINASE Insulinase family, zinc-binding region signature. GsryedsnnlGtSHLLRLAsSlTT
ChainResidueDetails
vGLY68-THR91
site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiACKlCEaVCP
ChainResidueDetails
HCYS113-PRO124
HCYS152-PRO163
site_idPS00535
Number of Residues12
DetailsCOMPLEX1_49K Respiratory chain NADH dehydrogenase 49 Kd subunit signature. LHRGtEKLiEyK
ChainResidueDetails
CLEU122-LYS133
site_idPS00542
Number of Residues22
DetailsCOMPLEX1_30K Respiratory chain NADH dehydrogenase 30 Kd subunit signature. EREiwDMFgvffanHpdlRrIL
ChainResidueDetails
DGLU167-LEU188
site_idPS00641
Number of Residues18
DetailsCOMPLEX1_75K_1 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 1. PrfCYherlsvaGnCRmC
ChainResidueDetails
GPRO61-CYS78
site_idPS00642
Number of Residues13
DetailsCOMPLEX1_75K_2 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 2. CPiCDqGGeCdLQ
ChainResidueDetails
GCYS128-GLN140
site_idPS00643
Number of Residues11
DetailsCOMPLEX1_75K_3 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 3. RCIqCtRCIrF
ChainResidueDetails
GARG175-PHE185
site_idPS00644
Number of Residues16
DetailsCOMPLEX1_51K_1 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 1. GAGAYICGEETALIES
ChainResidueDetails
BGLY200-SER215
site_idPS00645
Number of Residues12
DetailsCOMPLEX1_51K_2 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 2. ESCGqCtPCReG
ChainResidueDetails
BGLU377-GLY388
site_idPS00667
Number of Residues16
DetailsCOMPLEX1_ND1_1 Respiratory-chain NADH dehydrogenase subunit 1 signature 1. GLLQpIaDALKLFtKE
ChainResidueDetails
rGLY44-GLU59
site_idPS00668
Number of Residues14
DetailsCOMPLEX1_ND1_2 Respiratory-chain NADH dehydrogenase subunit 1 signature 2. PFDLTEGEseLVs.G
ChainResidueDetails
rPRO197-GLY210
site_idPS00848
Number of Residues23
DetailsCOX5B_1 Cytochrome c oxidase subunit Vb, zinc binding region signature. VIWfwvhkgetqrCpsCGthYKL
ChainResidueDetails
ApVAL100-LEU122
site_idPS01099
Number of Residues19
DetailsCOMPLEX1_24K Respiratory-chain NADH dehydrogenase 24 Kd subunit signature. DklFTlieveCLGaCvnAP
ChainResidueDetails
EASP166-PRO184
site_idPS01150
Number of Residues17
DetailsCOMPLEX1_20K Respiratory-chain NADH dehydrogenase 20 Kd subunit signature. GcDRIVPVDIYvPgCPP
ChainResidueDetails
IGLY152-PRO168
site_idPS01329
Number of Residues18
DetailsCOX6A Cytochrome c oxidase subunit VIa signature. IRtKpYsWGDGnHTlFhN
ChainResidueDetails
AqILE67-ASN84
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI17
Number of Residues1125
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues24
DetailsTopological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"UniProtKB","id":"P07470","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues28
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"UniProtKB","id":"P07470","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues16
DetailsTopological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"UniProtKB","id":"P00430","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues26
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"UniProtKB","id":"P00430","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P17665","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI35
Number of Residues47
DetailsTopological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI36
Number of Residues28
DetailsTransmembrane: {"description":"Helical; Name=I","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI37
Number of Residues80
DetailsTopological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI38
Number of Residues35
DetailsTransmembrane: {"description":"Helical; Name=II","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI39
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=III","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI40
Number of Residues29
DetailsTransmembrane: {"description":"Helical; Name=IV","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI41
Number of Residues29
DetailsTransmembrane: {"description":"Helical; Name=V","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI42
Number of Residues33
DetailsTransmembrane: {"description":"Helical; Name=VI","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI43
Number of Residues16
DetailsTransmembrane: {"description":"Helical; Name=VII","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI44
Number of Residues28
DetailsTransmembrane: {"description":"Helical; Name=VIII","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI45
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=IX","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI46
Number of Residues29
DetailsTransmembrane: {"description":"Helical; Name=X","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI47
Number of Residues26
DetailsTransmembrane: {"description":"Helical; Name=XI","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI48
Number of Residues31
DetailsTransmembrane: {"description":"Helical; Name=XII","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI49
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI50
Number of Residues3
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI51
Number of Residues2
DetailsCross-link: {"description":"1'-histidyl-3'-tyrosine (His-Tyr)","evidences":[{"source":"UniProtKB","id":"P00396","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI52
Number of Residues13
DetailsTopological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"UniProtKB","id":"P68530","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI53
Number of Residues30
DetailsTransmembrane: {"description":"Helical; Name=I","evidences":[{"source":"UniProtKB","id":"P68530","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI54
Number of Residues27
DetailsTransmembrane: {"description":"Helical; Name=II","evidences":[{"source":"UniProtKB","id":"P68530","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI55
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P68530","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI56
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P00406","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI57
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=I","evidences":[{"source":"UniProtKB","id":"P00415","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI58
Number of Residues37
DetailsTopological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"UniProtKB","id":"P00415","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI59
Number of Residues25
DetailsTransmembrane: {"description":"Helical; Name=II","evidences":[{"source":"UniProtKB","id":"P00415","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI60
Number of Residues15
DetailsTopological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"UniProtKB","id":"P00415","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI61
Number of Residues32
DetailsTransmembrane: {"description":"Helical; Name=III","evidences":[{"source":"UniProtKB","id":"P00415","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI62
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=IV","evidences":[{"source":"UniProtKB","id":"P00415","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI63
Number of Residues27
DetailsTransmembrane: {"description":"Helical; Name=V","evidences":[{"source":"UniProtKB","id":"P00415","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI64
Number of Residues32
DetailsTransmembrane: {"description":"Helical; Name=VI","evidences":[{"source":"UniProtKB","id":"P00415","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI65
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=VII","evidences":[{"source":"UniProtKB","id":"P00415","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI67
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00692","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI68
Number of Residues3
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P19536","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

238582

PDB entries from 2025-07-09

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