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2WD4

Ascorbate Peroxidase as a heme oxygenase: w41A variant product with t-butyl peroxide

Functional Information from GO Data
ChainGOidnamespacecontents
A0000302biological_processresponse to reactive oxygen species
A0004601molecular_functionperoxidase activity
A0006979biological_processresponse to oxidative stress
A0009507cellular_componentchloroplast
A0016688molecular_functionL-ascorbate peroxidase activity
A0020037molecular_functionheme binding
A0034599biological_processcellular response to oxidative stress
A0042744biological_processhydrogen peroxide catabolic process
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FE A 1250
ChainResidue
AHIS163
ATBV1253
AHOH2030

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 1251
ChainResidue
ATHR164
ATHR180
AASN182
AILE185
AASP187

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1252
ChainResidue
AGLY137
ASER138
AASP139
AHIS140
AHOH2184
ALYS136

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1254
ChainResidue
APRO127
APRO127
AARG130
AHOH2101
AHOH2185

site_idAC5
Number of Residues22
DetailsBINDING SITE FOR RESIDUE TBV A 1253
ChainResidue
APRO34
AALA41
AHIS42
APRO132
APHE145
ALEU159
ASER160
AHIS163
AILE165
AGLY166
AALA167
AALA168
AHIS169
AARG172
ASER173
ATRP179
ATYR235
AFE1250
AHOH2030
AHOH2187
AHOH2188
AHOH2189

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. DIVALSGGHTI
ChainResidueDetails
AASP155-ILE165

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1apx
ChainResidueDetails
AARG38
AHIS42
AASN71

222624

PDB entries from 2024-07-17

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