BioLiP

Structure of PDB 2fjm Chain B

Receptor sequence

>2fjmB (length=285) Species: 9606 (Homo sapiens) [Search protein sequence]

KLEFMEMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRY
RDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFW
EMVWEQKSRGVVMLNRVMEKCAQYWPQKEEKEMIFEDTNLKLTLISEDIK
SYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRE
SGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVL
LEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDS

3D structure

PDB

2fjm Conformation-assisted inhibition of protein-tyrosine phosphatase-1B elicits inhibitor selectivity over T-cell protein-tyrosine phosphatase.

Chain

Resolution

2.1 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	B	A518 D522 H525	A22 D26 H29	MOAD: ic50=142nM BindingDB: IC50=39nM
BS02	073	B	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 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

PDB	RCSB:2fjm, PDBe:2fjm, PDBj:2fjm
PDBsum	2fjm
PubMed	16407290
UniProt	P18031\|PTN1_HUMAN Tyrosine-protein phosphatase non-receptor type 1 (Gene Name=PTPN1)