Structure of PDB 5dj3 Chain B Binding Site BS02

Receptor Information
>5dj3 Chain B (length=351) Species: 141454 (Streptomyces wadayamensis) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LNIADGHARQALSPGQQKIVNELPVLWAESEQRPVQQIESEAHQAYFTLL
GQHGYPAEPGRVLSCYSSSVSMEILARSLSASVDRVALVHPTFDNIADLL
RGNGLDLVPVEEDALHGADLSAELLSSVGCVFVTTPNNPTGRVLAEERLR
RLAEQCAEHGTVLALDTSFRGFDAAAHYDHYAVLQEAGCRWVVIEDTGKL
WPTLDLKAGLLVFSEDIGLPVEKIYSDILLGVSPLILALIREFSRDAADG
GLADLHAFILHNRSVVRRALAGVEGVSFPDPESRSSVERVAFAGRTGTEV
WEELQRHHVFALPCRQFHWAEPSDGDHMVRIALSRSTEPLEKSVQVLRTV
L
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 chain5dj3 Chain B Residue 402 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB5dj3 Streptomyces wadayamensis MppP Is a Pyridoxal 5'-Phosphate-Dependent l-Arginine alpha-Deaminase, gamma-Hydroxylase in the Enduracididine Biosynthetic Pathway.
Resolution2.227 Å
Binding residue
(original residue number in PDB)
D116 D120
Binding residue
(residue number reindexed from 1)
D94 D98
Annotation score4
Enzymatic activity
Enzyme Commision number ?
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0046872 metal ion binding
Biological Process
GO:0006520 amino acid metabolic process
GO:0009058 biosynthetic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:5dj3, PDBe:5dj3, PDBj:5dj3
PDBsum5dj3
PubMed26551990
UniProtA0A0X1KHF5

[Back to BioLiP]