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3ZCG

Ascorbate peroxidase W41A-H42C 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 Residues21
DetailsBINDING SITE FOR RESIDUE HEM A 251
ChainResidue
APRO34
AALA167
AALA168
AHIS169
AARG172
ASER173
ATRP179
ASER207
ATYR235
AHOH2082
AHOH2230
AALA41
AHOH2312
AHOH2313
APRO132
AALA134
APHE145
ALEU159
AHIS163
AILE165
AGLY166

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 252
ChainResidue
APRO127
APRO127
AARG130
AHOH2192
AHOH2316
AHOH2317

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 1251
ChainResidue
ATHR164
ATHR180
AASN182
AILE185
AASP187
ASER189

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EPE A 1252
ChainResidue
ALYS30
ACYS32
ALEU80
AARG172
AHOH2312

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1253
ChainResidue
ALYS136
AGLY137
ASER138
AASP139
AHIS140
AHOH2202
AHOH2318

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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