Structure of PDB 2fjm Chain A

Receptor sequence
>2fjmA (length=285) Species: 9606 (Homo sapiens) [Search protein sequence]
KLEFMEMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRY
RDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFW
EMVWEQKSRGVVMLNRVMEKCAQYWPQKEEKEMIFEDTNLKLTLISEDIK
SYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRE
SGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVL
LEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDS
3D structure
PDB2fjm Conformation-assisted inhibition of protein-tyrosine phosphatase-1B elicits inhibitor selectivity over T-cell protein-tyrosine phosphatase.
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) D681 C715 R721 S722 Q762
Catalytic site (residue number reindexed from 1) D181 C215 R221 S222 Q262
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 073 A Y546 R547 D548 V549 F682 C715 S716 A717 I719 G720 R721 M758 Q762 Y50 R51 D52 V53 F182 C215 S216 A217 I219 G220 R221 M258 Q262 MOAD: ic50=142nM
PDBbind-CN: -logKd/Ki=6.85,IC50=142nM
BindingDB: IC50=39nM
BS02 073 A A518 H525 E526 A22 H29 E30 MOAD: ic50=142nM
PDBbind-CN: -logKd/Ki=6.85,IC50=142nM
BindingDB: IC50=39nM
Gene Ontology
Molecular Function
GO:0004725 protein tyrosine phosphatase activity
Biological Process
GO:0006470 protein dephosphorylation
GO:0016311 dephosphorylation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2fjm, PDBe:2fjm, PDBj:2fjm
PDBsum2fjm
PubMed16407290
UniProtP18031|PTN1_HUMAN Tyrosine-protein phosphatase non-receptor type 1 (Gene Name=PTPN1)

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