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1CRC

CYTOCHROME C AT LOW IONIC STRENGTH

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
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
A0020037molecular_functionheme binding
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0070069cellular_componentcytochrome complex
A0097190biological_processapoptotic signaling pathway
B0005515molecular_functionprotein binding
B0005758cellular_componentmitochondrial intermembrane space
B0005829cellular_componentcytosol
B0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
B0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
B0006915biological_processapoptotic process
B0008289molecular_functionlipid binding
B0009055molecular_functionelectron transfer activity
B0020037molecular_functionheme binding
B0042802molecular_functionidentical protein binding
B0046872molecular_functionmetal ion binding
B0070069cellular_componentcytochrome complex
B0097190biological_processapoptotic signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEC A 105
ChainResidue
ALYS13
ATHR49
AASN52
ATRP59
ATYR67
ATHR78
ALYS79
AMET80
AILE81
APHE82
AHOH107
ACYS14
AHOH110
ACYS17
AHIS18
AGLY29
APRO30
ATHR40
AGLY41
ATYR48

site_idAC2
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEC B 105
ChainResidue
ALYS55
BLYS13
BCYS14
BCYS17
BHIS18
BTHR28
BPRO30
BLEU32
BLEU35
BTHR40
BGLY41
BGLN42
BPHE46
BTYR48
BTHR49
BASN52
BTRP59
BTYR67
BTHR78
BLYS79
BMET80
BILE81
BPHE82
BHOH112

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBinding site: {"description":"covalent"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00433","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"5545094","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"description":"axial binding residue"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N-acetylglycine","evidences":[{"source":"PubMed","id":"14469771","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62894","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62897","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62897","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P62897","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

244349

PDB entries from 2025-11-05

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