Structure of PDB 2vo2 Chain X

Receptor sequence
>2vo2X (length=248) Species: 3847 (Glycine max) [Search protein sequence]
GKSYPTVSADYQKAVEKAKKKLRGFIAEKRCAPLMLRLAAHSAGTFDKGT
KTGGPFGTIKHPAELAHSANNGLDIAVRLLEPLKAEFPILSYADFYQLAG
VVAVEVTGGPEVPFHPGREDKPEPPPEGRLPDATKGSDHLRDVFGKAMGL
TDQDIVALSGGHTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLSGEKEG
LLQLPSDKALLSDPVFRPLVDKYAADEDAFFADYAEAHQKLSELGFAD
3D structure
PDB2vo2 Iron Oxidation State Modulates Active Site Structure in a Heme Peroxidase.
ChainX
Resolution1.9 Å
3D
structure
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Enzymatic activity
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 X P34 L37 A41 H42 P132 A134 L141 F145 L159 G162 H163 I165 G166 A167 A168 H169 R172 S173 W179 L205 S207 P33 L36 A40 H41 P131 A133 L140 F144 L158 G161 H162 I164 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:2vo2, PDBe:2vo2, PDBj:2vo2
PDBsum2vo2
PubMed18351739
UniProtQ43758

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