Structure of PDB 2cm8 Chain A

Receptor sequence
>2cm8A (length=297) Species: 9606 (Homo sapiens) [Search protein sequence]
EMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSP
FDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWE
QKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKS
YYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRES
GSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLL
EMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWKELSHED
3D structure
PDB2cm8 Structural Basis for Inhibition of Protein-Tyrosine Phosphatase 1B by Isothiazolidinone Heterocyclic Phosphonate Mimetics.
ChainA
Resolution2.1 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) D180 C214 R220 S221 Q261
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 F16 A Y46 D181 F182 C215 S216 A217 I219 G220 R221 Q262 D298 Y45 D180 F181 C214 S215 A216 I218 G219 R220 Q261 D297 MOAD: ic50=1350nM
PDBbind-CN: -logKd/Ki=5.87,IC50=1.35uM
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:2cm8, PDBe:2cm8, PDBj:2cm8
PDBsum2cm8
PubMed16916797
UniProtP18031|PTN1_HUMAN Tyrosine-protein phosphatase non-receptor type 1 (Gene Name=PTPN1)

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