Structure of PDB 1vkp Chain B Binding Site BS01

Receptor Information
>1vkp Chain B (length=363) Species: 3702 (Arabidopsis thaliana) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SPAEHGYYMPAEWDSHAQTWIGWPERQDNWRHNALPAQRVFAGVAKAISK
FEPVTVCASPAQWENARKQLPEDIRVVEMSMNDSWFRDSGPTFIVRKRNR
NIAGIDWNFNAWGGANDGCYNDWSHDLLVSRKILALERIPRFQHSMILEG
GSIHVDGEGTCLVTEECLLNKNRNPHMSKEQIEEELKKYLGVQSFIWLPR
GLYGDEDTNGHIDNMCCFARPGVVLLSWTDDETDPQYERSVEALSVLSNS
IDARGRKIQVIKLYIPEPLYMTEEESSGITQDGEAIPRLAGTRLAASYVN
FYIANGGIIAPQFGDPIRDKEAIRVLSDTFPHHSVVGIENAREIVLAGGN
IHCITQQQPAEPT
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain1vkp Chain B Residue 801 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1vkp X-ray Structure of Gene Product from Arabidopsis Thaliana At5g08170
Resolution1.53 Å
Binding residue
(original residue number in PDB)		D119 W120 S143
Binding residue
(residue number reindexed from 1)		D106 W107 S130
Annotation score1
Enzymatic activity
Enzyme Commision number 3.5.3.12: agmatine deiminase.
Gene Ontology
Molecular Function
GO:0004668 protein-arginine deiminase activity
GO:0016787 hydrolase activity
GO:0047632 agmatine deiminase activity
Biological Process
GO:0006596 polyamine biosynthetic process
GO:0009446 putrescine biosynthetic process
GO:0033388 putrescine biosynthetic process from arginine

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1vkp, PDBe:1vkp, PDBj:1vkp
PDBsum1vkp
PubMed
UniProtQ8GWW7|AGUA_ARATH Agmatine deiminase (Gene Name=AIH)

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