Structure of PDB 6bmx Chain B

Receptor sequence
>6bmxB (length=478) Species: 9606 (Homo sapiens) [Search protein sequence]
RRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDFTLSVRRNGAVTH
IKIQNTGDYYDLYGGEKFATLAELVQYYMEHHGQLKGDVIELKYPLNCAD
PTSERWFHGHLSGKEAEKLLTEKGKHGSFLVRESPGDFVLSVRTSKVTHV
MIRCQELKYDVGGGERFDSLTDLVEHYKKNPMVETLGTVLQLKQPLNTTR
INAAEIESRVRELSKGFWEEFETLQQQECKLLYSRKEGQRQENKNKNRYK
NILPFDHTRVVLHVSDYINANIIMPPKKSYIATQGCLQNTVNDFWRMVFQ
ENSRVIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYT
LRELKLSKVGQGNTERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHKQE
SIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMV
RSQRSGMVQTEAQYRFIYMAVQHYIETL
3D structure
PDB6bmx Dual Allosteric Inhibition of SHP2 Phosphatase.
ChainB
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) D378 C412 R418 T419 Q459
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 B Q79 Y80 E83 H84 L262 Y263 S264 R265 K266 Q269 N281 L283 Q76 Y77 E80 H81 L232 Y233 S234 R235 K236 Q239 N251 L253
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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