Structure of PDB 5ehp Chain B

Receptor sequence
>5ehpB (length=471) Species: 9606 (Homo sapiens) [Search protein sequence]
RRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDFTLSVRRNGAVTH
IKIQNTGDYYDLYGGEKFATLAELVQYYMEQLKDVIELKYPLNCADPTSE
RWFHGHLSGKEAEKLLTEKGKHGSFLVRESDFVLSVRTSKVTHVMIRCQE
LKYDVGGGERFDSLTDLVEHYKKNPMVETLGTVLQLKQPLNTTRINAAEI
ESRVRELSKQGFWEEFETLQQQECKLLYSRKEGQRQENKNKNRYKNILPF
DHTRVVLHVSDYINANIIMPKSYIATQGCLQNTVNDFWRMVFQENSRVIV
MTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYTLRELKLS
KVGQGNTERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHKQESIMDAGP
VVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGM
VQTEAQYRFIYMAVQHYIETL
3D structure
PDB5ehp Allosteric Inhibition of SHP2: Identification of a Potent, Selective, and Orally Efficacious Phosphatase Inhibitor.
ChainB
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D425 C459 R465 T466 Q506
Catalytic site (residue number reindexed from 1) D371 C405 R411 T412 Q452
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 5OA B R111 F113 H114 T219 E249 E250 T253 L254 Q257 P491 K492 Q495 R101 F103 H104 T193 E214 E215 T218 L219 Q222 P437 K438 Q441 MOAD: ic50=12uM
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:5ehp, PDBe:5ehp, PDBj:5ehp
PDBsum5ehp
PubMed27347692
UniProtQ06124|PTN11_HUMAN Tyrosine-protein phosphatase non-receptor type 11 (Gene Name=PTPN11)

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