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1IYN

Crystal structure of chloroplastic ascorbate peroxidase from tobacco plants and structural insights for its instability

Functional Information from GO Data
ChainGOidnamespacecontents
A0000302biological_processresponse to reactive oxygen species
A0004601molecular_functionperoxidase activity
A0006979biological_processresponse to oxidative stress
A0009507cellular_componentchloroplast
A0016491molecular_functionoxidoreductase activity
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
A0140825molecular_functionlactoperoxidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 297
ChainResidue
ATHR164
ATHR196
AGLN198
ALYS201
AHOH312

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 298
ChainResidue
AHOH306
AASP35
AGLY51
AASN53
ASER55

site_idAC3
Number of Residues24
DetailsBINDING SITE FOR RESIDUE HEM A 296
ChainResidue
APRO26
AARG30
ATRP33
APRO131
AASP132
AALA133
ALEU142
APHE146
ALEU159
AALA162
AHIS163
AGLY166
AARG167
ASER168
AARG169
AARG172
ASER173
ATRP195
ATHR223
ATYR251
AHOH299
AHOH305
AHOH325
AHOH363

Functional Information from PROSITE/UniProt
site_idPS00435
Number of Residues11
DetailsPEROXIDASE_1 Peroxidases proximal heme-ligand signature. EIVALSGAHTL
ChainResidueDetails
AGLU155-LEU165

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1apx
ChainResidueDetails
AHIS34
AARG30
AASN67

246333

PDB entries from 2025-12-17

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