Structure of PDB 4h2b Chain A

Receptor sequence
>4h2bA (length=524) Species: 9606 (Homo sapiens) [Search protein sequence]
PWELTILHTNDVHSRLEQTSEDSSKCVDASRCMGGVARLFTKVQQIRRAE
PNVLLLDAGDQYQGTIWFTVYKGAEVAHFMNALRYDAMALGNHEFDNGVE
GLIEPLLKEAKFPILSANISASGPLASQISGLYLPYKVLPVGDEVVGIVG
YTSKETPFLSNPGTNLVFEDEITALQPEVDKLKTLNVNKIIALGHSGFEM
DKLIAQKVRGVDVVVGGHSNTFLYTGNPPSKEVPAGKYPFIVTSDDGRKV
PVVQAYAFGKYLGYLKIEFDERGNVISSHGNPILLDSSIPEDPSIKADIN
KWRIKLDDYSTQELGKTIVYLDGSSQSCRFRECNMGNLICDAMINNNLRH
ADEMFWNHVSMCILNGGGIRSPIDERNDGTITWENLAAVLPFGGTFDLVQ
LKGSTLKKAFEHSVHRYGQSTGEFLQVGGIHVVYDLSRKPGDRVVKLDVL
CTSCRVPSYDPLKMDEVYKVILPNFLANGGDGFQMIKDELLRHDSGDQDI
NVVSTYISKMKVIYPAVEGRIKFS
3D structure
PDB4h2b Crystal Structure of the Human Ecto-5'-Nucleotidase (CD73): Insights into the Regulation of Purinergic Signaling.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D36 H38 D85 N117 H118 D121 H220 H243 N245 S350 R354 R395
Catalytic site (residue number reindexed from 1) D11 H13 D60 N92 H93 D96 H195 H218 N220 S325 R329 R370
Enzyme Commision number 3.1.3.35: thymidylate 5'-phosphatase.
3.1.3.5: 5'-nucleotidase.
3.1.3.89: 5'-deoxynucleotidase.
3.1.3.91: 7-methylguanosine nucleotidase.
3.1.3.99: IMP-specific 5'-nucleotidase.
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 ZN A D85 N117 H220 H243 D60 N92 H195 H218
BS02 ZN A D36 H38 D85 D11 H13 D60
BS03 0XE A D47 R354 N390 G392 G393 R395 F417 G447 F500 D506 D22 R329 N365 G367 G368 R370 F392 G422 F475 D481
BS04 CA A N213 D237 G298 N188 D212 G273
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0002953 5'-deoxynucleotidase activity
GO:0005515 protein binding
GO:0008252 nucleotidase activity
GO:0008253 5'-nucleotidase activity
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0016788 hydrolase activity, acting on ester bonds
GO:0042802 identical protein binding
GO:0046872 metal ion binding
GO:0050340 thymidylate 5'-phosphatase activity
GO:0050483 IMP 5'-nucleotidase activity
GO:0050484 GMP 5'-nucleotidase activity
GO:0106411 XMP 5'-nucleosidase activity
Biological Process
GO:0006196 AMP catabolic process
GO:0006259 DNA metabolic process
GO:0007159 leukocyte cell-cell adhesion
GO:0009166 nucleotide catabolic process
GO:0033198 response to ATP
GO:0046032 ADP catabolic process
GO:0046034 ATP metabolic process
GO:0046086 adenosine biosynthetic process
GO:0050728 negative regulation of inflammatory response
GO:0055074 calcium ion homeostasis
GO:0140928 inhibition of non-skeletal tissue mineralization
Cellular Component
GO:0005654 nucleoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0009897 external side of plasma membrane
GO:0009986 cell surface
GO:0016020 membrane
GO:0070062 extracellular exosome
GO:0098552 side of membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4h2b, PDBe:4h2b, PDBj:4h2b
PDBsum4h2b
PubMed23142347
UniProtP21589|5NTD_HUMAN 5'-nucleotidase (Gene Name=NT5E)

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