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5L86

engineered ascorbate peroxidise

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
B0000302biological_processresponse to reactive oxygen species
B0004601molecular_functionperoxidase activity
B0006979biological_processresponse to oxidative stress
B0009507cellular_componentchloroplast
B0016688molecular_functionL-ascorbate peroxidase activity
B0020037molecular_functionheme binding
B0034599biological_processcellular response to oxidative stress
B0042744biological_processhydrogen peroxide catabolic process
B0046872molecular_functionmetal ion binding
B0098869biological_processcellular oxidant detoxification
Functional Information from PDB Data
site_idAC1
Number of Residues20
Detailsbinding site for residue HEM A 301
ChainResidue
APRO34
AALA168
AHIS169
AARG172
ASER173
ATRP179
ASER207
ATYR235
AHOH410
AHOH428
AHOH442
APHE41
AHOH517
APRO132
APRO134
APHE145
ALEU159
AMHS163
AGLY166
AALA167

site_idAC2
Number of Residues6
Detailsbinding site for residue SO4 A 302
ChainResidue
ALYS20
AARG24
ALYS112
AHOH404
AHOH493
BLYS112

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 303
ChainResidue
AGLY137
ASER138
AASP139
AHIS140

site_idAC4
Number of Residues3
Detailsbinding site for residue SO4 A 304
ChainResidue
AARG31
ALEU184
AHOH494

site_idAC5
Number of Residues21
Detailsbinding site for residue HEM B 301
ChainResidue
BPRO34
BARG38
BPHE41
BPRO132
BPRO134
BPHE145
BLEU159
BMHS163
BGLY166
BALA167
BALA168
BHIS169
BARG172
BSER173
BTRP179
BSER207
BTYR235
BHOH431
BHOH433
BHOH443
BHOH484

site_idAC6
Number of Residues5
Detailsbinding site for residue SO4 B 302
ChainResidue
ALYS112
BLYS20
BARG24
BLYS112
BHOH418

site_idAC7
Number of Residues6
Detailsbinding site for residue SO4 B 303
ChainResidue
BLYS136
BGLY137
BSER138
BASP139
BHIS140
BHOH506

site_idAC8
Number of Residues2
Detailsbinding site for residue SO4 B 304
ChainResidue
BARG31
BHOH485

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. APlmLRLaFHSA
ChainResidueDetails
AALA33-ALA44

221371

PDB entries from 2024-06-19

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