Structure of PDB 6bmv Chain A

Receptor sequence
>6bmvA (length=483) Species: 9606 (Homo sapiens) [Search protein sequence]
SRRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDFTLSVRRNGAVT
HIKIQNTGDYYDLYGGEKFATLAELVQYYMEHHGQLKNGDVIELKYPLNC
ADPTSERWFHGHLSGKEAEKLLTEKGKHGSFLVRESQPGDFVLSVRTGSK
VTHVMIRCQELKYDVGGGERFDSLTDLVEHYKKNPMVETLGTVLQLKQPL
NTTRINAAEIESRVRELSKQGFWEEFETLQQQECKLLYSRKEGQRQENKN
KNRYKNILPFDHTRVVLHPVSDYINANIIMPEKSYIATQGCLQNTVNDFW
RMVFQENSRVIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESA
AHDYTLRELKLSKVGQGNTERTVWQYHFRTWPDHGVPSDPGGVLDFLEEV
HHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPK
TIQMVRSQRSGMVQTEAQYRFIYMAVQHYIETL
3D structure
PDB6bmv Dual Allosteric Inhibition of SHP2 Phosphatase.
ChainA
Resolution2.053 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) D383 C417 R423 T424 Q464
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 DZS A Q79 Y80 E83 H84 L262 Y263 S264 R265 K266 Q269 N281 Q77 Y78 E81 H82 L237 Y238 S239 R240 K241 Q244 N256 PDBbind-CN: -logKd/Ki=4.68,IC50=21uM
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:6bmv, PDBe:6bmv, PDBj:6bmv
PDBsum6bmv
PubMed29304282
UniProtQ06124|PTN11_HUMAN Tyrosine-protein phosphatase non-receptor type 11 (Gene Name=PTPN11)

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