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2XJ6

The structure of ferrous ascorbate peroxidase

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 Residues21
DetailsBINDING SITE FOR RESIDUE HEM A 1001
ChainResidue
APRO34
AALA167
AALA168
AHIS169
AARG172
ASER173
ATRP179
ASER207
ATYR235
AHOH2080
AHOH2082
ATRP41
AHOH2330
AHOH2331
APRO132
AALA134
APHE145
ALEU159
AHIS163
AILE165
AGLY166

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 1002
ChainResidue
APRO127
APRO127
AARG130
AHOH2332
AHOH2333

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 1003
ChainResidue
AGLY137
ASER138
AASP139
AHIS140
AHOH2221
AHOH2334
AHOH2335
AHOH2336

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 2751
ChainResidue
ATHR164
ATHR180
AASN182
AILE185
AASP187

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

site_idPS00436
Number of Residues12
DetailsPEROXIDASE_2 Peroxidases active site signature. APlmLRLaWHSA
ChainResidueDetails
AALA33-ALA44

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PDB entries from 2024-07-24

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