Structure of PDB 5ehp Chain A

Receptor sequence
>5ehpA (length=494) Species: 9606 (Homo sapiens) [Search protein sequence]
SRRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDFTLSVRRNGAVT
HIKIQNTGDYYDLYGGEKFATLAELVQYYMEHQLKEKNGDVIELKYPLNC
ADPTSERWFHGHLSGEAEKLLTEKGKHGSFLVRESSHPGDFVLSVRTGSK
VTHVMIRCQELKYDVGGGERFDSLTDLVEHYKKNPMVELGTVLQLKQPLN
TTRINAAEIESRVRELSKLAKQGFWEEFETLQQQECKLLYSRKEGQRQEN
KNKNRYKNILPFDHTRVVLHDGPNEPVSDYINANIIMPEFKPKKSYIATQ
GCLQNTVNDFWRMVFQENSRVIVMTTKEVERGKSKCVKYWPDEYALKEYG
VMRVRNVKESAAHDYTLRELKLSKVGQGNTERTVWQYHFRTWPDHGVPSD
PGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIRE
KGVDCDIDVPKTIQMVRSQRSGMVQTEAQYRFIYMAVQHYIETL
3D structure
PDB5ehp Allosteric Inhibition of SHP2: Identification of a Potent, Selective, and Orally Efficacious Phosphatase Inhibitor.
ChainA
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) D394 C428 R434 T435 Q475
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 A R111 F113 H114 T219 E249 T253 L254 Q257 P491 K492 Q495 R107 F109 H110 T202 E226 T230 L231 Q234 P460 K461 Q464 MOAD: ic50=12uM
PDBbind-CN: -logKd/Ki=4.92,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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