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3WUI

Dimeric horse cytochrome c formed by refolding from molten globule state

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005758cellular_componentmitochondrial intermembrane space
A0005829cellular_componentcytosol
A0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
A0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
A0006915biological_processapoptotic process
A0008289molecular_functionlipid binding
A0009055molecular_functionelectron transfer activity
A0018063biological_processcytochrome c-heme linkage
A0020037molecular_functionheme binding
A0042802molecular_functionidentical protein binding
A0043065biological_processpositive regulation of apoptotic process
A0043280biological_processpositive regulation of cysteine-type endopeptidase activity involved in apoptotic process
A0046872molecular_functionmetal ion binding
A0070069cellular_componentcytochrome complex
A0070469cellular_componentrespirasome
A2001056biological_processpositive regulation of cysteine-type endopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE HEM A 201
ChainResidue
ALYS13
ATYR48
ATHR49
AASN52
ATRP59
ALEU64
ATYR67
ALEU68
ATHR78
ALYS79
AMET80
ACYS14
AALA83
APEG204
AHOH310
AHOH315
ACYS17
AHIS18
ATHR28
AGLY29
APRO30
ATHR40
AGLY41

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PG4 A 202
ChainResidue
ALYS55
ALYS55
AGLU66
ALYS73
ALYS73
ATYR74
ATYR74
APRO76
APRO76

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 203
ChainResidue
ALYS7
ATYR97
ATYR97
ALYS100
ALYS100
AGLU104
AGLU104
AHOH321
AHOH321

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PEG A 204
ChainResidue
ATHR47
ATYR48
ATHR49
ALYS79
AHEC201

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PEG A 205
ChainResidue
AGLN16
AGLN16

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: covalent
ChainResidueDetails
ACYS17
ACYS14

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:5545094
ChainResidueDetails
AHIS18

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: axial binding residue
ChainResidueDetails
AMET80

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N-acetylglycine => ECO:0000269|PubMed:14469771
ChainResidueDetails
AGLY1

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P62894
ChainResidueDetails
ATYR97
ATYR48

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P62897
ChainResidueDetails
ALYS55

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897
ChainResidueDetails
ALYS72

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P62897
ChainResidueDetails
ALYS99

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PDB entries from 2024-05-15

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