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3ZCH

Ascorbate peroxidase W41A-H42M mutant

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 Residues23
DetailsBINDING SITE FOR RESIDUE HEM A 251
ChainResidue
APRO34
AILE165
AGLY166
AALA167
AALA168
AHIS169
AARG172
ASER173
ATRP179
ASER207
ATYR235
AARG38
AEPE1251
AHOH2189
AHOH2259
AHOH2260
AALA41
APRO132
AALA134
APHE145
ALEU159
AGLY162
AHIS163

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 252
ChainResidue
AGLU124
APRO127
APRO127
AGLU128
AARG130

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 253
ChainResidue
ALYS136
AGLY137
ASER138
AASP139
AHIS140
AHOH2157

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EPE A 1251
ChainResidue
AARG38
AALA41
AMET42
ALEU131
APRO132
AHEM251
AHOH2151

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EPE A 1252
ChainResidue
ALYS30
AARG31
AARG172
AHOH2260

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 1253
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

221051

PDB entries from 2024-06-12

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