Structure of PDB 6mdc Chain A

Receptor sequence
>6mdcA (length=483) Species: 9606 (Homo sapiens) [Search protein sequence]
RRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDFTLSVRRNGAVTH
IKIQNTGDYYDLYGGEKFATLAELVQYYMEHIELKYPLNCADPTSERWFH
GHLSGKEAEKLLTEKGKHGSFLVRESGDFVLSVRTGDSKVTHVMIRCQEL
KYDVGGGERFDSLTDLVEHYKKNPMVETLGTVLQLKQPLNTTRINAAEIE
SRVRELSKLQGFWEEFETLQQQECKLLYSRKEGQRQENKNKNRYKNILPF
DHTRVVLHDGDPNEPVSDYINANIIMPEFKPKKSYIATQGCLQNTVNDFW
RMVFQENSRVIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESA
AHDYTLRELKLSKVGQGNTERTVWQYHFRTWPDHGVPSDPGGVLDFLEEV
HHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPK
TIQMVRSQRSGMVQTEAQYRFIYMAVQHYIETL
3D structure
PDB6mdc Optimization of Fused Bicyclic Allosteric SHP2 Inhibitors.
ChainA
Resolution2.14 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 JEA A T108 E110 R111 F113 T219 E249 E250 T253 L254 Q257 P491 K492 T94 E96 R97 F99 T192 E214 E215 T218 L219 Q222 P449 K450 MOAD: ic50=0.036uM
PDBbind-CN: -logKd/Ki=7.44,IC50=0.036uM
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:6mdc, PDBe:6mdc, PDBj:6mdc
PDBsum6mdc
PubMed30688462
UniProtQ06124|PTN11_HUMAN Tyrosine-protein phosphatase non-receptor type 11 (Gene Name=PTPN11)

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