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3E2N

Engineering ascorbate peroxidase activity into 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
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE HEM A 296
ChainResidue
APRO37
AHIS168
AGLY171
ALYS172
ATHR173
AHIS174
AARG177
ASER178
ALEU225
ATHR227
AHOH1054
AARG41
AHOH1126
AHOH1215
AHOH1370
ATRP44
APRO138
AASP139
AALA140
ALEU164
AMET165
AALA167

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. EVVALMGAHAL
ChainResidueDetails
AGLU160-LEU170

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. GPvlVRLaWHTS
ChainResidueDetails
AGLY36-SER47

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor
ChainResidueDetails
AHIS45

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Tryptophan radical intermediate => ECO:0000269|PubMed:2851317
ChainResidueDetails
APHE184

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
AHIS168

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Transition state stabilizer
ChainResidueDetails
AARG41

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ATYR146

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1apx
ChainResidueDetails
AASN75
AHIS45
AARG41

site_idMCSA1
Number of Residues3
DetailsM-CSA 709
ChainResidueDetails
AARG41electrostatic stabiliser
AHIS45electrostatic stabiliser, proton acceptor, proton donor
APHE184single electron acceptor, single electron donor

site_idMCSA2
Number of Residues
DetailsM-CSA 399
ChainResidueDetails

229380

PDB entries from 2024-12-25

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