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2B0Z

Crystal structure of the protein-protein complex between F82I cytochrome c and cytochrome c peroxidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0006979biological_processresponse to oxidative stress
A0020037molecular_functionheme binding
A0034599biological_processcellular response to oxidative stress
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
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ZNH A 295
ChainResidue
APRO44
AGLY178
ALYS179
ATHR180
AHIS181
AASN184
ASER185
ATRP191
ATHR234
APHE266
AVAL45
AVAL47
AARG48
ATRP51
ALEU171
AMET172
AALA174
AHIS175

site_idAC2
Number of Residues19
DetailsBINDING SITE FOR RESIDUE HEC B 109
ChainResidue
BARG13
BCYS14
BCYS17
BHIS18
BVAL28
BILE35
BSER40
BGLY41
BTYR46
BTYR48
BTHR49
BASN52
BTRP59
BMET64
BTYR67
BTHR78
BLYS79
BMET80
BILE82

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. EVVALMGAHAL
ChainResidueDetails
AGLU167-LEU177

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. GPvlVRLaWHTS
ChainResidueDetails
AGLY43-SER54

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: covalent => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5
ChainResidueDetails
BLEU15
BHIS18

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:11880631, ECO:0000269|PubMed:18390544, ECO:0007744|PDB:1KYO, ECO:0007744|PDB:3CX5
ChainResidueDetails
BTHR19
BALA81

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6,N6,N6-trimethyllysine; by CTM1 => ECO:0000269|PubMed:10791961, ECO:0000269|PubMed:11880631, ECO:0007744|PDB:1KYO
ChainResidueDetails
BLYS73

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:10821864, ECO:0000269|PubMed:18390544
ChainResidueDetails
BTYR74

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ATYR153

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1apx
ChainResidueDetails
AARG48
AHIS52
AASN82

site_idMCSA1
Number of Residues3
DetailsM-CSA 709
ChainResidueDetails
AARG48electrostatic stabiliser
AHIS52electrostatic stabiliser, proton acceptor, proton donor
ATRP191single electron acceptor, single electron donor

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PDB entries from 2024-07-24

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