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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
DetailsActive site: {"description":"Proton acceptor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Tryptophan radical intermediate","evidences":[{"source":"PubMed","id":"2851317","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00297","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7703247","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7703247","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1APX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

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 Residues5
DetailsM-CSA 399
ChainResidueDetails
AARG41transition state stabiliser
AHIS45proton shuttle (general acid/base)
AHIS168activator, metal ligand
APHE184radical stabiliser
AASP228activator

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PDB entries from 2025-12-03

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