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4QAO

Lysine-ligated cytochrome c with F82H

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
B0005515molecular_functionprotein binding
B0005739cellular_componentmitochondrion
B0005758cellular_componentmitochondrial intermembrane space
B0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
B0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
B0009055molecular_functionelectron transfer activity
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
B0070469cellular_componentrespirasome
B1901612molecular_functioncardiolipin binding
C0005515molecular_functionprotein binding
C0005739cellular_componentmitochondrion
C0005758cellular_componentmitochondrial intermembrane space
C0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
C0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
C0009055molecular_functionelectron transfer activity
C0020037molecular_functionheme binding
C0046872molecular_functionmetal ion binding
C0070469cellular_componentrespirasome
C1901612molecular_functioncardiolipin binding
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM A 201
ChainResidue
ACYS14
ATYR46
ATYR48
ATHR49
AASP50
ATRP59
ATYR67
ALYS73
AILE75
APRO76
AGLY77
ACYS17
AALA81
AHIS82
AHOH301
AHOH303
AHOH312
AHIS18
AVAL28
APRO30
ALEU32
AILE35
ASER40
AGLY41

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE HEM B 201
ChainResidue
BARG13
BCYS14
BCYS17
BHIS18
BVAL28
BILE35
BSER40
BGLY41
BTYR46
BTYR48
BTHR49
BASP50
BTRP59
BTYR67
BLYS73
BPRO76
BGLY83
BLEU94
BHOH305
BHOH307

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM C 201
ChainResidue
CARG13
CCYS14
CCYS17
CHIS18
CVAL28
CILE35
CSER40
CGLY41
CTYR46
CTYR48
CTHR49
CASP50
CILE53
CTRP59
CMET64
CTYR67
CLYS73
CILE75
CPRO76
CGLY77
CALA81
CHOH303
CHOH341
CHOH342

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5
ChainResidueDetails
ACYS14
ACYS17
BCYS14
BCYS17
CCYS14
CCYS17

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5
ChainResidueDetails
AHIS18
AMET80
BHIS18
BMET80
CHIS18
CMET80

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: N6,N6,N6-trimethyllysine; by CTM1 => ECO:0000269|PubMed:10791961, ECO:0000269|PubMed:11880631, ECO:0007744|PDB:1KYO
ChainResidueDetails
AALA72
BALA72
CALA72

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:10821864, ECO:0000269|PubMed:18390544
ChainResidueDetails
ALYS73
BLYS73
CLYS73

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PDB entries from 2024-05-01

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