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2XIF

The structure of ascorbate peroxidase Compound II

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 Residues25
DetailsBINDING SITE FOR RESIDUE HEM A 1251
ChainResidue
APRO34
AHIS163
AILE165
AGLY166
AALA167
AALA168
AHIS169
AARG172
ASER173
ALEU205
ASER207
AARG38
ATYR235
AHOH2131
AHOH2512
AHOH2513
AHOH2514
AHOH2515
ATRP41
APRO132
AALA134
APHE145
ALEU159
ASER160
AGLY162

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1252
ChainResidue
APRO127
AARG130
AHOH2516
AHOH2517
AHOH2518
AHOH2520

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 1253
ChainResidue
ALYS136
AGLY137
ASER138
AASP139
AHIS140
AHOH2361
AHOH2521
AHOH2522
AHOH2523
AHOH2524

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 1254
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

221371

PDB entries from 2024-06-19

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