Structure of PDB 3vpb Chain B Binding Site BS03

Receptor Information
>3vpb Chain B (length=282) Species: 273063 (Sulfurisphaera tokodaii str. 7) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MRVVLIVDIVRQEEKLIAKALEENKVQYDIINVAQEPLPFNKALGRYDVA
IIRPVSMYRALYSSAVLEAAGVHTINSSDVINVCGDKILTYSKLYREGIP
IPDSIIALSAEAALKAYEQRGFPLIDKPPIGSWGRLVSLIRDVFEGKTII
EHRELMGNSALKAHIVQEYIQYKGRDIRCIAIGEELLGCYARNIPPNEWR
ANVALGGTPSNIEVDEKLKETVVKAVSIVHGEFVSIDILEHPNKGYVVNE
LNDVPEFKGFMVATNINVAQKLVEYIKENYSK
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 chain3vpb Chain B Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3vpb Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus
Resolution1.8 Å
Binding residue
(original residue number in PDB)
D237 E250
Binding residue
(residue number reindexed from 1)
D237 E250
Annotation score1
Enzymatic activity
Enzyme Commision number 6.3.2.-
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0042802 identical protein binding
GO:0043774 coenzyme F420-2 alpha-glutamyl ligase activity
GO:0046872 metal ion binding
Biological Process
GO:0006526 L-arginine biosynthetic process
GO:0009085 lysine biosynthetic process
GO:0036211 protein modification process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:3vpb, PDBe:3vpb, PDBj:3vpb
PDBsum3vpb
PubMed23434852
UniProtQ970U6|ARGX_SULTO Glutamate--LysW ligase ArgX (Gene Name=argX)

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