Structure of PDB 5ven Chain B Binding Site BS02

Receptor Information
>5ven Chain B (length=373) Species: 10090 (Mus musculus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
QKVLVVSFDGFRWDYLYKVPTPHFHYIMKNGVHVNQVTNVFITKTYPNHY
TLVTGLFAENHGIVANDMFDPILNKSFSLEHMDIYDSKFWEEATPIWITN
QRAGHASGAAMWPGADVKIHDSFPTYYLPYNESVSFEDRVAKIIEWFTAK
DPINLGFLYWEEPDDTGHDVGPDSPLMGSVISDVDHKLGYLIKMLKRAKL
WNNVNLIVTSDHGMTQCSKQRVIELDRYLDKEHYTLIDHSPVAAILPKEG
KFDEVYDALAGAHPNLTVYKKEEIPERWHYKHNDRVQPIVAVADEGWYIL
QNKSDDFLLGNHGYDNALAEMHPIFLAHGPAFRKNFTKEAMNSTDLYSLL
CHLLNLTALPHNGSFWNVQDLLS
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain5ven Chain B Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB5ven A key tyrosine substitution restricts nucleotide hydrolysis by the ectoenzyme NPP5.
Resolution1.69 Å
Binding residue
(original residue number in PDB)		D191 H195 H339
Binding residue
(residue number reindexed from 1)		D164 H168 H312
Annotation score1
Enzymatic activity
Enzyme Commision number 3.1.-.-
Gene Ontology
Molecular Function
GO:0000210 NAD+ diphosphatase activity
GO:0004551 dinucleotide phosphatase activity
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0007154 cell communication
GO:0009166 nucleotide catabolic process
Cellular Component
GO:0005576 extracellular region
GO:0005886 plasma membrane
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5ven, PDBe:5ven, PDBj:5ven
PDBsum5ven
PubMed28898552
UniProtQ9EQG7|ENPP5_MOUSE Ectonucleotide pyrophosphatase/phosphodiesterase family member 5 (Gene Name=Enpp5)

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