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2Y6A

Ascorbate Peroxidase R38A 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
AALA167
AALA168
AHIS169
AARG172
ASER173
ATRP179
ALEU205
ASER207
ATYR235
AHOH2274
ATRP41
AHOH2369
AHOH2370
AHOH2371
AHOH2372
APRO132
AALA134
ALEU141
ALEU159
AHIS163
AILE165
AGLY166

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1250
ChainResidue
APRO127
APRO127
AARG130
AHOH2226
AHOH2231
AHOH2373
AHOH2374

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 1251
ChainResidue
ALYS136
AGLY137
ASER138
AASP139
AHIS140
AHOH2252
AHOH2375
AHOH2376
AHOH2377
AHOH2378

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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