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5DFS

Crystal structure of Spider Monkey Cytochrome C at 1.15 Angstrom

Functional Information from GO Data
ChainGOidnamespacecontents
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
A0009055molecular_functionelectron transfer activity
A0020037molecular_functionheme binding
A0043280biological_processpositive regulation of cysteine-type endopeptidase activity involved in apoptotic process
A0046872molecular_functionmetal ion 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
B0009055molecular_functionelectron transfer activity
B0020037molecular_functionheme binding
B0043280biological_processpositive regulation of cysteine-type endopeptidase activity involved in apoptotic process
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues21
Detailsbinding site for residue HEC A 201
ChainResidue
ALYS13
ATYR48
ATHR49
AASN52
ATRP59
ATYR67
ATHR78
ALYS79
AMET80
AILE81
APHE82
ACYS14
AHOH334
BLYS55
ACYS17
AHIS18
ATHR28
AGLY29
APRO30
ATHR40
AGLY41

site_idAC2
Number of Residues2
Detailsbinding site for residue EDO A 202
ChainResidue
AGLY1
AHOH326

site_idAC3
Number of Residues4
Detailsbinding site for residue EDO A 203
ChainResidue
ALYS55
AHOH301
AHOH306
AHOH409

site_idAC4
Number of Residues2
Detailsbinding site for residue CL A 204
ChainResidue
AGLU61
ALYS99

site_idAC5
Number of Residues3
Detailsbinding site for residue CL A 205
ChainResidue
AGLU50
AHOH395
AHOH422

site_idAC6
Number of Residues4
Detailsbinding site for residue EDO B 202
ChainResidue
ALYS39
BLYS13
BHOH304
BHOH375

site_idAC7
Number of Residues3
Detailsbinding site for residue EDO B 203
ChainResidue
BLYS87
BLYS88
BGLU89

site_idAC8
Number of Residues4
Detailsbinding site for residue EDO B 204
ChainResidue
BLYS25
BHOH312
BHOH315
BHOH381

site_idAC9
Number of Residues5
Detailsbinding site for residue EDO B 205
ChainResidue
BGLY60
BGLU61
BLYS99
BHOH306
BHOH310

site_idAD1
Number of Residues23
Detailsbinding site for Di-peptide HEM B 201 and CYS B 17
ChainResidue
BLYS13
BCYS14
BSER15
BGLN16
BHIS18
BLYS27
BTHR28
BGLY29
BPRO30
BTHR40
BGLY41
BTYR48
BTHR49
BASN52
BTRP59
BTYR67
BTHR78
BLYS79
BMET80
BILE81
BPHE82
BHOH347
BHOH362

site_idAD2
Number of Residues23
Detailsbinding site for Di-peptide HEM B 201 and CYS B 14
ChainResidue
BPHE10
BLYS13
BSER15
BGLN16
BCYS17
BHIS18
BTHR28
BGLY29
BPRO30
BTHR40
BGLY41
BTYR48
BTHR49
BASN52
BTRP59
BTYR67
BTHR78
BLYS79
BMET80
BILE81
BPHE82
BHOH347
BHOH362

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: covalent
ChainResidueDetails
ACYS14
ACYS17
BCYS14
BCYS17

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: axial binding residue
ChainResidueDetails
AHIS18
AMET80
BHIS18
BMET80

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylglycine => ECO:0000250|UniProtKB:P62894, ECO:0000305
ChainResidueDetails
AGLY1
BGLY1

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P62894
ChainResidueDetails
ATYR48
ATYR97
BTYR48
BTYR97

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P62897
ChainResidueDetails
ALYS55
BLYS55

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62897
ChainResidueDetails
ALYS72
BLYS72

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P62897
ChainResidueDetails
ALYS99
BLYS99

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PDB entries from 2024-10-30

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