Structure of PDB 6bmx Chain A

Receptor sequence
>6bmxA (length=488) Species: 9606 (Homo sapiens) [Search protein sequence]
SRRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDFTLSVRRNGAVT
HIKIQNTGDYYDLYGGEKFATLAELVQYYMEHHGQLKENGDVIELKYPLN
CADPTSERWFHGHLSGKEAEKLLTEKGKHGSFLVRESPGDFVLSVRTGSK
VTHVMIRCQELKYDVGGGERFDSLTDLVEHYKKNPMVETLGTVLQLKQPL
NTTRINAAEIESRVRELSKLQGFWEEFETLQQQECKLLYSRKEGQRQENK
NKNRYKNILPFDHTRVVLHDGDPPVSDYINANIIMPEKSYIATQGCLQNT
VNDFWRMVFQENSRVIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRN
VKESAAHDYTLRELKLSKVGQGNTERTVWQYHFRTWPDHGVPSDPGGVLD
FLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCD
IDVPKTIQMVRSQRSGMVQTEAQYRFIYMAVQHYIETL
3D structure
PDB6bmx Dual Allosteric Inhibition of SHP2 Phosphatase.
ChainA
Resolution2.424 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) D388 C422 R428 T429 Q469
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 DYV A Q79 Y80 E83 H84 L262 Y263 S264 R265 K266 Q269 K280 N281 Q77 Y78 E81 H82 L238 Y239 S240 R241 K242 Q245 K256 N257 PDBbind-CN: -logKd/Ki=4.72,IC50=18.9uM
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:6bmx, PDBe:6bmx, PDBj:6bmx
PDBsum6bmx
PubMed29304282
UniProtQ06124|PTN11_HUMAN Tyrosine-protein phosphatase non-receptor type 11 (Gene Name=PTPN11)

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