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1MK8

Crystal Structure of a Mutant Cytochrome c Peroxidase showing a Novel Trp-Tyr Covalent Cross-link

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 Residues24
DetailsBINDING SITE FOR RESIDUE HEM A 296
ChainResidue
APRO44
AHIS175
ALEU177
AGLY178
ALYS179
ATHR180
AHIS181
AASN184
ASER185
ATRP191
ALEU232
AVAL45
ATHR234
AHOH324
AHOH325
AHOH340
AHOH899
ATRP51
ATYR52
APRO145
AASP146
ALEU171
AMET172
AALA174

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
ATYR52

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Tryptophan radical intermediate => ECO:0000269|PubMed:2851317
ChainResidueDetails
ATRP191

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_idMCSA1
Number of Residues3
DetailsM-CSA 709
ChainResidueDetails
AARG48electrostatic stabiliser
ATYR52electrostatic stabiliser, proton acceptor, proton donor
ATRP191single electron acceptor, single electron donor

226707

PDB entries from 2024-10-30

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