Structure of PDB 5veo Chain A

Receptor sequence
>5veoA (length=374) Species: 10090 (Mus musculus) [Search protein sequence]
EQKVLVVSFDGFRWDYLYKVPTPHFHYIMKNGVHVNQVTNVFITKAYPNH
YTLVTGLFAENHGIVANDMFDPILNKSFSLEHMDIYDSKFWEEATPIWIT
NQRAGHASGAAMWPGADVKIHDSFPTYYLPYNESVSFEDRVAKIIEWFTA
KDPINLGFLYWEEPDDTGHDVGPDSPLMGSVISDVDHKLGYLIKMLKRAK
LWNNVNLIVTSDHGMTQCSKQRVIELDRYLDKEHYTLIDHSPVAAILPKE
GKFDEVYDALAGAHPNLTVYKKEEIPERWHYKHNDRVQPIVAVADEGWYI
LQNKSDDFLLGNHGYDNALAEMHPIFLAHGPAFRKNFTKEAMNSTDLYSL
LCHLLNLTALPHNGSFWNVQDLLS
3D structure
PDB5veo A key tyrosine substitution restricts nucleotide hydrolysis by the ectoenzyme NPP5.
ChainA
Resolution1.53 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.1.-.-
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 FUC A K102 S103 K76 S77
BS02 ZN A D191 H195 H339 D165 H169 H313
BS03 ZN A D36 D238 H239 D10 D212 H213
BS04 ZN A E159 D192 E133 D166
BS05 AMP A D36 A72 Y73 L106 M109 Y157 E159 Y186 E188 H339 D10 A46 Y47 L80 M83 Y131 E133 Y160 E162 H313
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:5veo, PDBe:5veo, PDBj:5veo
PDBsum5veo
PubMed28898552
UniProtQ9EQG7|ENPP5_MOUSE Ectonucleotide pyrophosphatase/phosphodiesterase family member 5 (Gene Name=Enpp5)

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