Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2XIH

The structure of ascorbate peroxidase Compound III

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 Residues24
DetailsBINDING SITE FOR RESIDUE HEM A 1251
ChainResidue
APRO34
AILE165
AGLY166
AALA167
AALA168
AHIS169
AARG172
ASER173
ATRP179
ASER207
ATYR235
AARG38
AOXY1254
AHOH2121
AHOH2472
AHOH2473
AHOH2474
ATRP41
APRO132
AALA134
APHE145
ALEU159
AGLY162
AHIS163

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 A 1252
ChainResidue
ALYS136
AGLY137
ASER138
AASP139
AHIS140
AHOH2326
AHOH2475
AHOH2476
AHOH2478

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 1253
ChainResidue
ATHR164
ATHR180
AASN182
AILE185
AASP187

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OXY A 1254
ChainResidue
AARG38
ATRP41
AHIS42
AHEM1251
AHOH2121
AHOH2479

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

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon