Structure of PDB 1q6n Chain B

Receptor sequence
>1q6nB (length=289) Species: 9606 (Homo sapiens) [Search protein sequence]
KLEFMEMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRY
RDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFW
EMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLIS
EDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLF
KVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDI
KKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDS
3D structure
PDB1q6n The Structural Basis for the Selectivity of Benzotriazole Inhibitors of Ptp1B
ChainB
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) D1181 C1215 R1221 S1222 Q1262
Catalytic site (residue number reindexed from 1) D185 C219 R225 S226 Q266
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 P90 B D1022 H1025 E1026 D26 H29 E30 MOAD: ic50=0.023uM
BS02 P90 B Y1046 R1047 D1048 K1120 F1182 C1215 S1216 A1217 I1219 G1220 R1221 M1258 Q1262 Y50 R51 D52 K124 F186 C219 S220 A221 I223 G224 R225 M262 Q266 MOAD: ic50=0.023uM
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:1q6n, PDBe:1q6n, PDBj:1q6n
PDBsum1q6n
PubMed14516196
UniProtP18031|PTN1_HUMAN Tyrosine-protein phosphatase non-receptor type 1 (Gene Name=PTPN1)

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