Structure of PDB 1q6p Chain B

Receptor sequence
>1q6pB (length=287) Species: 9606 (Homo sapiens) [Search protein sequence]
KLEFMEMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRY
RDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFW
EMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLIS
EDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLF
KVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDI
KKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMG
3D structure
PDB1q6p The Structural Basis for the Selectivity of Benzotriazole Inhibitors of Ptp1B
ChainB
Resolution2.3 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 213 B A1018 Q1021 R1024 A22 Q25 R28 MOAD: ic50=3nM
BindingDB: IC50=3nM
BS02 213 B R1024 Y1046 R1047 D1048 L1119 F1182 C1215 S1216 A1217 I1219 G1220 R1221 R1254 M1258 Q1262 R28 Y50 R51 D52 L123 F186 C219 S220 A221 I223 G224 R225 R258 M262 Q266 MOAD: ic50=3nM
BindingDB: IC50=3nM
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:1q6p, PDBe:1q6p, PDBj:1q6p
PDBsum1q6p
PubMed14516196
UniProtP18031|PTN1_HUMAN Tyrosine-protein phosphatase non-receptor type 1 (Gene Name=PTPN1)

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