Structure of PDB 1oag Chain A

Receptor sequence
>1oagA (length=249) Species: 3847 (Glycine max) [Search protein sequence]
GKSYPTVSADYQKAVEKAKKKLRGFIAEKRCAPLMLRLAWHSAGTFDKGT
KTGGPFGTIKHPAELAHSANNGLDIAVRLLEPLKAEFPILSYADFYQLAG
VVAVEVTGGPEVPFHPGREDKPEPPPEGRLPDATKGSDHLRDVFGKAMGL
TDQDIVALSGGHTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLSGEKEG
LLQLPSDKALLSDPVFRPLVDKYAADEDAFFADYAEAHQKLSELGFADA
3D structure
PDB1oag Crystal Structure of the Ascorbate Peroxidase-Ascorbate Complex
ChainA
Resolution1.75 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R38 H42 L66 H163 W179 D208
Catalytic site (residue number reindexed from 1) R37 H41 L65 H162 W178 D207
Enzyme Commision number 1.11.1.11: L-ascorbate peroxidase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 HEM A P34 R38 W41 P132 A134 L141 F145 L159 H163 G166 A167 A168 H169 R172 S173 W179 L205 S207 P33 R37 W40 P131 A133 L140 F144 L158 H162 G165 A166 A167 H168 R171 S172 W178 L204 S206
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0016688 L-ascorbate peroxidase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0006979 response to oxidative stress
GO:0034599 cellular response to oxidative stress
GO:0098869 cellular oxidant detoxification

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Molecular Function
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Biological Process
External links
PDB RCSB:1oag, PDBe:1oag, PDBj:1oag
PDBsum1oag
PubMed12640445
UniProtQ43758

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