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6P43

Yeast cytochrome c peroxidase in complex with iso-1 cytochrome c (Y48K)

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
B1901612molecular_functioncardiolipin binding
C0004601molecular_functionperoxidase activity
C0006979biological_processresponse to oxidative stress
C0020037molecular_functionheme binding
C0034599biological_processcellular response to oxidative stress
Functional Information from PDB Data
site_idAC1
Number of Residues24
Detailsbinding site for residue HEM A 301
ChainResidue
APRO44
AHIS175
ALEU177
AGLY178
ALYS179
ATHR180
AHIS181
AASN184
ASER185
ATRP191
ALEU232
AVAL45
ATHR234
AHOH440
AHOH493
AHOH500
AHOH534
AARG48
ATRP51
AASP146
AALA147
ALEU171
AMET172
AALA174

site_idAC2
Number of Residues22
Detailsbinding site for residue HEM B 201
ChainResidue
AALA193
AALA194
BARG13
BCYS14
BGLN16
BCYS17
BHIS18
BVAL28
BLEU32
BSER40
BGLY41
BTYR46
BLYS48
BTHR49
BTRP59
BMET64
BTYR67
BLEU68
BTHR78
BLYS79
BMET80
BLEU94

site_idAC3
Number of Residues21
Detailsbinding site for residue HEM C 301
ChainResidue
CPRO44
CARG48
CTRP51
CPRO145
CALA147
CLEU171
CALA174
CHIS175
CLEU177
CGLY178
CLYS179
CTHR180
CHIS181
CASN184
CSER185
CTRP191
CLEU232
CTHR234
CHOH486
CHOH491
CHOH560

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. GPvlVRLaWHIS
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
BCYS14
BCYS17

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
BHIS18
BMET80

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
BLYS72
CHIS175

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6,N6,N6-trimethyllysine => ECO:0000269|PubMed:10821864, ECO:0000269|PubMed:18390544
ChainResidueDetails
BLYS73
CARG48

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ATYR153
CTYR153

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

site_idMCSA2
Number of Residues3
DetailsM-CSA 709
ChainResidueDetails
CARG48electrostatic stabiliser
CHIS52electrostatic stabiliser, proton acceptor, proton donor
CTRP191single electron acceptor, single electron donor

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PDB entries from 2025-06-11

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