Structure of PDB 2ghk Chain X

Receptor sequence
>2ghkX (length=250) Species: 3847 (Glycine max) [Search protein sequence]
SGKSYPTVSADYQKAVEKAKKKLRGFIAEKRCAPLMLRLAWHSAGTFDKG
TKTGGPFGTIKHPAELAHSANNGLDIAVRLLEPLKAEFPILSYADFYQLA
GVVAVEVTGGPEVPFHPGREDKPEPPPEGRLPDATKGSDHLRDVFGKAMG
LTDQDIVALSGGHTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLSGEKE
GLLQLPSDKALLSDPVFRPLVDKYAADEDAFFADYAEAHQKLSELGFADA
3D structure
PDB2ghk Conformational Mobility in the Active Site of a Heme Peroxidase.
ChainX
Resolution1.999 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 R38 W41 P132 A134 F145 L159 G162 H163 G166 A167 A168 H169 R172 S173 W179 L205 S207 P34 R38 W41 P132 A134 F145 L159 G162 H163 G166 A167 A168 H169 R172 S173 W179 L205 S207
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:2ghk, PDBe:2ghk, PDBj:2ghk
PDBsum2ghk
PubMed16762924
UniProtQ43758

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