Structure of PDB 5kad Chain A

Receptor sequence
>5kadA (length=285) Species: 9606 (Homo sapiens) [Search protein sequence]
HMASMEMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRY
RDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFW
EMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLIS
EDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLAFLF
KVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDI
KKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFI
3D structure
PDB5kad Conformational Rigidity and Protein Dynamics at Distinct Timescales Regulate PTP1B Activity and Allostery.
ChainA
Resolution1.9 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 OTA A Y46 D48 K120 D181 F182 C215 S216 A217 I219 G220 R221 Q262 Y50 D52 K124 D185 F186 C219 S220 A221 I223 G224 R225 Q266 MOAD: Kd=37uM
PDBbind-CN: -logKd/Ki=4.43,Kd=37uM
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:5kad, PDBe:5kad, PDBj:5kad
PDBsum5kad
PubMed28212750
UniProtP18031|PTN1_HUMAN Tyrosine-protein phosphatase non-receptor type 1 (Gene Name=PTPN1)

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