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1YIC

THE OXIDIZED SACCHAROMYCES CEREVISIAE ISO-1-CYTOCHROME C, NMR, 20 STRUCTURES

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005758cellular_componentmitochondrial intermembrane space
A0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
A0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
A0009055molecular_functionelectron transfer activity
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
A0070469cellular_componentrespirasome
A1901612molecular_functioncardiolipin binding
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEC A 104
ChainResidue
AARG13
AGLY41
ATYR46
ATYR48
ATHR49
AASN52
ATRP59
AMET64
ATYR67
ALEU68
ATHR78
ACYS14
ALYS79
AMET80
AALA81
APHE82
ALEU85
ALEU94
ACYS17
AHIS18
AVAL28
AGLY29
ALEU32
AILE35
ASER40

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5
ChainResidueDetails
ALEU15
AHIS18

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5
ChainResidueDetails
ATHR19
AALA81

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6,N6,N6-trimethyllysine; by CTM1 => ECO:0000269|PubMed:10791961, ECO:0000269|PubMed:11880631, ECO:0007744|PDB:1KYO
ChainResidueDetails
ALYS73

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:10821864, ECO:0000269|PubMed:18390544
ChainResidueDetails
ATYR74

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PDB entries from 2024-05-01

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