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3O20

Electron transfer complexes:experimental mapping of the Redox-dependent Cytochrome C electrostatic surface

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
B0005515molecular_functionprotein binding
B0005739cellular_componentmitochondrion
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
B0018063biological_processcytochrome c-heme linkage
B0020037molecular_functionheme binding
B0042802molecular_functionidentical protein binding
B0043065biological_processpositive regulation of apoptotic process
B0043280biological_processpositive regulation of cysteine-type endopeptidase activity involved in apoptotic process
B0046872molecular_functionmetal ion binding
B0070069cellular_componentcytochrome complex
B0070469cellular_componentrespirasome
B2001056biological_processpositive regulation of cysteine-type endopeptidase activity
C0005515molecular_functionprotein binding
C0005739cellular_componentmitochondrion
C0005758cellular_componentmitochondrial intermembrane space
C0005829cellular_componentcytosol
C0006122biological_processmitochondrial electron transport, ubiquinol to cytochrome c
C0006123biological_processmitochondrial electron transport, cytochrome c to oxygen
C0006915biological_processapoptotic process
C0008289molecular_functionlipid binding
C0009055molecular_functionelectron transfer activity
C0018063biological_processcytochrome c-heme linkage
C0020037molecular_functionheme binding
C0042802molecular_functionidentical protein binding
C0043065biological_processpositive regulation of apoptotic process
C0043280biological_processpositive regulation of cysteine-type endopeptidase activity involved in apoptotic process
C0046872molecular_functionmetal ion binding
C0070069cellular_componentcytochrome complex
C0070469cellular_componentrespirasome
C2001056biological_processpositive regulation of cysteine-type endopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEC A 105
ChainResidue
ALYS13
ATYR48
ATHR49
AASN52
ATRP59
ALEU64
ATYR67
ALEU68
ATHR78
ALYS79
AMET80
ACYS14
AILE81
APHE82
ALEU94
AHOH131
AHOH211
ACYS17
AHIS18
ATHR28
AGLY29
APRO30
ATHR40
AGLY41

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 A 106
ChainResidue
AVAL11
AHOH141
AHOH168
CPHE82
CALA83
CGLY84

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 A 107
ChainResidue
APHE82
AALA83
AGLY84
AHOH179
BLYS8
BVAL11
BGLN12

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NO3 A 108
ChainResidue
ALYS13
AGLY84
ALYS86
ALYS87
AGLU90

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 A 109
ChainResidue
ATHR19
AVAL20
AGLU21
AHOH236
CTHR28
CILE81
CHOH124

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 A 110
ChainResidue
ATHR28
AILE81
AHOH178
BPHE10
BTHR19
BVAL20
BGLU21

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE NO3 A 111
ChainResidue
AGLY77
AHOH132
AHOH261
CLYS39
CILE57
CTHR58
CLYS60
CTHR63

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 A 112
ChainResidue
AGLY45
APHE46
ATHR47
AHOH118
AHOH180
BLYS53

site_idAC9
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEC B 105
ChainResidue
BLYS13
BCYS14
BGLN16
BCYS17
BHIS18
BTHR28
BGLY29
BPRO30
BTHR40
BGLY41
BTYR48
BTHR49
BASN52
BTRP59
BLEU64
BTYR67
BLEU68
BTHR78
BLYS79
BMET80
BILE81
BPHE82
BLEU94
BHOH119
BHOH135

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 B 106
ChainResidue
BTHR47
BHOH276
CLYS25
ALYS53
BHIS26
BGLY45
BPHE46

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NO3 B 107
ChainResidue
BLYS27
BTHR28
BNO3111
CLYS25
CLYS27

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 B 108
ChainResidue
BPHE82
BALA83
BGLY84
BHOH147
BHOH332
CVAL11

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 B 109
ChainResidue
BLYS13
BGLY84
BILE85
BLYS86
BHOH163
CLYS8

site_idBC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE NO3 B 110
ChainResidue
BLYS39
BGLY56
BILE57
BTHR58
BLYS60
BTHR63
BHOH194
BHOH355
CGLY77
CHOH196

site_idBC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NO3 B 111
ChainResidue
ALYS25
AHIS26
ALYS27
ATHR28
AHOH347
BLYS25
BLYS27
BNO3107
BHOH133

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 B 112
ChainResidue
ALYS100
BPHE36
BLYS60
BGLU61
BLYS99
BHOH136

site_idBC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE NO3 B 113
ChainResidue
ALYS39
AGLY56
AILE57
ATHR58
ALYS60
AHOH142
BGLY77
BHOH263
BHOH354

site_idBC9
Number of Residues26
DetailsBINDING SITE FOR RESIDUE HEC C 105
ChainResidue
AALA15
CLYS13
CCYS14
CCYS17
CHIS18
CTHR28
CGLY29
CPRO30
CTHR40
CGLY41
CPHE46
CTYR48
CTHR49
CASN52
CTRP59
CTYR67
CLEU68
CTHR78
CLYS79
CMET80
CILE81
CPHE82
CLEU98
CHOH121
CHOH124
CHOH136

site_idCC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NO3 C 106
ChainResidue
AGLU4
ALYS7
CLYS72
CALA83

site_idCC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 C 107
ChainResidue
BTHR28
BILE81
CTHR19
CVAL20
CGLU21
CHOH117
CHOH318

site_idCC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 C 108
ChainResidue
ALYS8
AHOH351
CLYS13
CGLY84
CILE85
CLYS86
CHOH345

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBINDING: covalent
ChainResidueDetails
ACYS14
ACYS17
BCYS14
BCYS17
CCYS14
CCYS17

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: axial binding residue => ECO:0000255|PROSITE-ProRule:PRU00433, ECO:0000269|PubMed:5545094
ChainResidueDetails
AHIS18
BHIS18
CHIS18

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: axial binding residue
ChainResidueDetails
AMET80
BMET80
CMET80

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: N-acetylglycine => ECO:0000269|PubMed:14469771
ChainResidueDetails
AGLY1
BGLY1
CGLY1

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P62894
ChainResidueDetails
ATYR48
ATYR97
BTYR48
BTYR97
CTYR48
CTYR97

site_idSWS_FT_FI6
Number of Residues3
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P62897
ChainResidueDetails
ALYS55
BLYS55
CLYS55

site_idSWS_FT_FI7
Number of Residues3
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897
ChainResidueDetails
ALYS72
BLYS72
CLYS72

site_idSWS_FT_FI8
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P62897
ChainResidueDetails
ALYS99
BLYS99
CLYS99

218853

PDB entries from 2024-04-24

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