Structure of PDB 1v0h Chain X Binding Site BS02

Receptor Information
>1v0h Chain X (length=249) Species: 3847 (Glycine max) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SGKSYPTVSADYQKAVEKAKKKLRGFIAEKRCAPLMLRLAWHSAGTFDKG
TKTGGPFGTIKHPAELAHSANNGLDIAVRLLEPLKAEFPILSYADFYQLA
GVVAVEVTGGPEVPFHPGREDKPEPPPEGRLPDATKGSDHLRDVFGKAMG
LTDQDIVALSGGHTIGAAHKERSGFEGPWTSNPLIFDNSYFTELLSGEKE
GLLQLPSDKALLSDPVFRPLVDKYAADEDAFFADYAEAHQKLSELGFAD
Ligand information
Ligand IDSHA
InChIInChI=1S/C7H7NO3/c9-6-4-2-1-3-5(6)7(10)8-11/h1-4,9,11H,(H,8,10)
InChIKeyHBROZNQEVUILML-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1ccc(c(c1)C(=O)NO)O
ACDLabs 10.04O=C(c1ccccc1O)NO
CACTVS 3.341ONC(=O)c1ccccc1O
FormulaC7 H7 N O3
NameSALICYLHYDROXAMIC ACID
ChEMBLCHEMBL309339
DrugBankDB03819
ZINCZINC000018169763
PDB chain1v0h Chain X Residue 253 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1v0h Crystal Structure of the Ascorbate Peroxidase-Salicylhydroxamic Acid Complex
Resolution1.46 Å
Binding residue
(original residue number in PDB)		R38 W41 H42 A70 P132
Binding residue
(residue number reindexed from 1)		R38 W41 H42 A70 P132
Annotation score1
Enzymatic activity
Enzyme Commision number 1.11.1.11: L-ascorbate peroxidase.
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:1v0h, PDBe:1v0h, PDBj:1v0h
PDBsum1v0h
PubMed15236572
UniProtQ43758

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