Structure of PDB 2vew Chain A

Receptor sequence
>2vewA (length=296) Species: 9606 (Homo sapiens) [Search protein sequence]
MEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPF
DHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQ
KSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSY
YTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESG
SLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLE
MRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWKELSHED
3D structure
PDB2vew Isothiazolidinone Inhibitors of Ptp1B Containing Imidazoles and Imidazolines
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D181 C215 R221 S222 Q262
Catalytic site (residue number reindexed from 1) D179 C213 R219 S220 Q260
Enzyme Commision number 3.1.3.48: protein-tyrosine-phosphatase.
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 IZ3 A Y46 D48 V49 D181 F182 C215 S216 A217 I219 G220 R221 D298 Y44 D46 V47 D179 F180 C213 S214 A215 I217 G218 R219 D296 MOAD: ic50=64nM
PDBbind-CN: -logKd/Ki=7.19,IC50=64nM
Gene Ontology
Molecular Function
GO:0004725 protein tyrosine phosphatase activity
Biological Process
GO:0006470 protein dephosphorylation
GO:0016311 dephosphorylation

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Molecular Function
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Biological Process
External links
PDB RCSB:2vew, PDBe:2vew, PDBj:2vew
PDBsum2vew
PubMed18037290
UniProtP18031|PTN1_HUMAN Tyrosine-protein phosphatase non-receptor type 1 (Gene Name=PTPN1)

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