Structure of PDB 1q6j Chain A

Receptor sequence
>1q6jA (length=289) Species: 9606 (Homo sapiens) [Search protein sequence]
KLEFMEMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRY
RDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFW
EMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLIS
EDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLF
KVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDI
KKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDS
3D structure
PDB1q6j The Structural Basis for the Selectivity of Benzotriazole Inhibitors of Ptp1B
ChainA
Resolution2.2 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) 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 335 A Y46 R47 D48 V49 S118 L119 F182 C215 S216 A217 I219 G220 R221 Q262 Y50 R51 D52 V53 S122 L123 F186 C219 S220 A221 I223 G224 R225 Q266 MOAD: ic50=0.016uM
PDBbind-CN: -logKd/Ki=7.80,IC50=0.016uM
BindingDB: IC50=16nM
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
View graph for
Biological Process
External links
PDB RCSB:1q6j, PDBe:1q6j, PDBj:1q6j
PDBsum1q6j
PubMed14516196
UniProtP18031|PTN1_HUMAN Tyrosine-protein phosphatase non-receptor type 1 (Gene Name=PTPN1)

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