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2XI6

The structure of ascorbate peroxidase Compound I

Functional Information from GO Data
ChainGOidnamespacecontents
A0004601molecular_functionperoxidase activity
A0006979biological_processresponse to oxidative stress
A0016688molecular_functionL-ascorbate peroxidase activity
A0020037molecular_functionheme binding
A0034599biological_processcellular response to oxidative stress
A0046872molecular_functionmetal ion binding
A0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM A 288
ChainResidue
APRO34
AGLY166
AALA167
AALA168
AHIS169
AARG172
ASER173
ATRP179
ALEU205
ASER207
ATYR235
AARG38
AHOH2106
AHOH2107
AHOH2454
AHOH2455
AHOH2456
ATRP41
APRO132
AALA134
APHE145
ALEU159
AHIS163
AILE165

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 749
ChainResidue
APRO127
AARG130
AHOH2457
AHOH2458
AHOH2459
AHOH2460

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 750
ChainResidue
ALYS136
AGLY137
ASER138
AASP139
AHIS140
AHOH2461
AHOH2463

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 751
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 2024-09-04

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