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3EXB

Crystal structure of Cytochrome C Peroxidase with a Proposed Electron Pathway Excised in a Complex with a Peptide Wire

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0006979biological_processresponse to oxidative stress
A0020037molecular_functionheme binding
A0034599biological_processcellular response to oxidative stress
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE HEM A 300
ChainResidue
APRO44
AALA174
AHIS175
ALEU177
AGLY178
ALYS179
ATHR180
AHIS181
AASN184
ASER185
ALEU230
AVAL45
ATHR232
AHOH584
AHOH710
AHOH860
AHOH884
BEXB293
AARG48
ATRP51
APRO145
AASP146
AALA147
ALEU171
AMET172

site_idAC2
Number of Residues15
DetailsBINDING SITE FOR CHAIN B OF N-[3-(1H-BENZIMIDAZOL-1-YL)PROPANOYL]GLYCYL-L-ALANYL-L- ALANINAMIDE
ChainResidue
AHIS175
ALEU177
AGLY178
ALYS179
AGLY191
AALA192
AASN193
AGLU199
ATYR227
AMET228
AASP233
AHEM300
AHOH529
AHOH651
AHOH809

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 Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS52

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Tryptophan radical intermediate => ECO:0000269|PubMed:2851317
ChainResidueDetails
AGLY191

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: axial binding residue => ECO:0000269|PubMed:10722697, ECO:0000269|PubMed:11170452, ECO:0000269|PubMed:2169873, ECO:0000269|PubMed:6092361, ECO:0000269|PubMed:8384877, ECO:0000269|PubMed:8673607
ChainResidueDetails
AHIS175

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AARG48

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
AGLY191single electron acceptor, single electron donor

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PDB entries from 2024-10-30

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