Structure of PDB 5ka3 Chain A

Receptor sequence
>5ka3A (length=295) Species: 9606 (Homo sapiens) [Search protein sequence]
EMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSP
FDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWE
QKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKS
AATVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRES
GSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLL
EMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWKELSH
3D structure
PDB5ka3 Conformational Rigidity and Protein Dynamics at Distinct Timescales Regulate PTP1B Activity and Allostery.
ChainA
Resolution2.141 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) D180 C214 R220 S221 Q261
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 OTA A Y46 D48 K120 D181 F182 C215 S216 A217 I219 G220 R221 Y45 D47 K119 D180 F181 C214 S215 A216 I218 G219 R220 MOAD: Kd=26uM
PDBbind-CN: -logKd/Ki=4.59,Kd=26uM
BindingDB: IC50=500000nM,Ki=11500nM
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
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Biological Process
External links
PDB RCSB:5ka3, PDBe:5ka3, PDBj:5ka3
PDBsum5ka3
PubMed28212750
UniProtP18031|PTN1_HUMAN Tyrosine-protein phosphatase non-receptor type 1 (Gene Name=PTPN1)

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