Structure of PDB 2shp Chain B

Receptor sequence
>2shpB (length=491) Species: 9606 (Homo sapiens) [Search protein sequence]
KSRRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDLTLSVRRNGAV
THIKIQNTGDYYDLYGGEKFATLAELVQYYMEHHGQLKEKNGDVIELKYP
LNCADPTSERWFHGHLSGKEAEKLLTEKGKHGSFLVRESQSHPGDFVLSV
RTGDNDGKSKVTHVMIRCQELKYDVGGGERFDSLTDLVEHYKKNPMVETL
GTVLQLKQPLNTTRINAAEIESRVRELSKGFWEEFETLQQQECKLLYSRK
EGQRQENKNKNRYKNILPFDHTRVVLHDSDYINANIIMPKKSYIATQGCL
QNTVNDFWRMVFQENSRVIVMTTKEVERGKSKCVKYWPDEYALKEYGVMR
VRNVKESAAHDYTLRELKLSKVGQGNTERTVWQYHFRTWPDHGVPSDPGG
VLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGV
DCDIDVPKTIQMVRSQRSGMVQTEAQYRSIYMAVQHYIETL
3D structure
PDB2shp Crystal structure of the tyrosine phosphatase SHP-2.
ChainB
Resolution2.0 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) D391 C425 R431 T432 Q472
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 CAT B F420 W423 P429 P432 V435 F438 F469 S513 M516 F386 W389 P395 P398 V401 F404 F435 S479 M482
Gene Ontology
Molecular Function
GO:0004725 protein tyrosine phosphatase activity
Biological Process
GO:0006470 protein dephosphorylation
GO:0016311 dephosphorylation

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2shp, PDBe:2shp, PDBj:2shp
PDBsum2shp
PubMed9491886
UniProtQ06124|PTN11_HUMAN Tyrosine-protein phosphatase non-receptor type 11 (Gene Name=PTPN11)

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