Structure of PDB 1lqf Chain D

Receptor sequence
>1lqfD (length=287) Species: 9606 (Homo sapiens) [Search protein sequence]
KLEFMEMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRY
RDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFW
EMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLIS
EDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLF
KVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDI
KKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMG
3D structure
PDB1lqf The structure of PTP-1B in complex with a peptide inhibitor reveals an alternative binding mode for bisphosphonates.
ChainD
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) D681 C715 R721 S722 Q762
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 BGD D R545 Y546 R547 D548 L619 K620 F682 C715 S716 A717 I719 G720 R721 R49 Y50 R51 D52 L123 K124 F186 C219 S220 A221 I223 G224 R225
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:1lqf, PDBe:1lqf, PDBj:1lqf
PDBsum1lqf
PubMed12119018
UniProtP18031|PTN1_HUMAN Tyrosine-protein phosphatase non-receptor type 1 (Gene Name=PTPN1)

[Back to BioLiP]