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4Q5P

Lysine-Ligated Yeast Iso-1 Cytochrome C

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 Residues25
DetailsBINDING SITE FOR RESIDUE HEM A 201
ChainResidue
AARG13
ATYR48
ATHR49
AASP50
ATRP59
AMET64
ATYR67
ALEU68
ALYS73
AILE75
APRO76
ACYS14
APHE82
ALEU94
AHOH304
AHOH305
AHOH310
AHOH313
AGLN16
ACYS17
AHIS18
AVAL28
ASER40
AGLY41
ATYR46

site_idAC2
Number of Residues26
DetailsBINDING SITE FOR RESIDUE HEM B 201
ChainResidue
BCYS14
BCYS17
BHIS18
BVAL28
BPRO30
BLEU32
BILE35
BSER40
BGLY41
BTYR46
BTYR48
BTHR49
BASP50
BTRP59
BTYR67
BLEU68
BLYS73
BGLY77
BALA81
BGLY83
BLEU85
BLEU94
BHOH303
BHOH305
BHOH307
BHOH308

site_idAC3
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM C 201
ChainResidue
CCYS14
CCYS17
CHIS18
CVAL28
CSER40
CGLY41
CTYR46
CTYR48
CTHR49
CASP50
CTRP59
CMET64
CTYR67
CLEU68
CLYS73
CILE75
CGLY77
CALA81
CPHE82
CGLY83
CLEU94
CHOH302
CHOH305
CHOH306
CHOH318

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 2024-07-24

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