Structure of PDB 5ehr Chain B

Receptor sequence
>5ehrB (length=470) Species: 9606 (Homo sapiens) [Search protein sequence]
RRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDFTLSVRRNGAVTH
IKIQNTGDYYDLYGGEKFATLAELVQYYMEIELKYPLNCADPTSERWFHG
HLSGKEAEKLLTEKGKHGSFLVRESSHPGDFVLSVRTSKVTHVMIRCQEL
KYDVGGGERFDSLTDLVEHYKKNPMVETLGTVLQLKQPLNTTRINAAEIE
SRVRELSKQGFWEEFETLQQQECKLLYSRKEGQRQENKNKNRYKNILPFD
HTRVVLHVSDYINANIIMPKSYIATQGCLQNTVNDFWRMVFQENSRVIVM
TTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYTLRELKLSK
VGQGNTERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHKQESIMDAGPV
VVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMV
QTEAQYRFIYMAVQHYIETL
3D structure
PDB5ehr Allosteric inhibition of SHP2 phosphatase inhibits cancers driven by receptor tyrosine kinases.
ChainB
Resolution1.7 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) D370 C404 R410 T411 Q451
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 5OD B E110 R111 F113 T219 E250 T253 L254 Q257 P491 K492 Q495 E95 R96 F98 T192 E214 T217 L218 Q221 P436 K437 Q440 MOAD: Kd=73nM
BindingDB: IC50=70.0nM
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:5ehr, PDBe:5ehr, PDBj:5ehr
PDBsum5ehr
PubMed27362227
UniProtQ06124|PTN11_HUMAN Tyrosine-protein phosphatase non-receptor type 11 (Gene Name=PTPN11)

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