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Ligands
Code Name Style Show Link
JJY 3,4,6,7-tetrahydroacridine-1,8(2h,5h)-dione
TRS 2-amino-2-hydroxymethyl-propane-1,3-diol
Non-standard Residues
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Code : 5QFP   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : PanDDA analysis group deposition -- Crystal structure of PTP1B in complex with compound_FMOMB000293a
Release Data : 2018-10-10
Compound :
mol_id molecule chains synonym
1 Tyrosine-protein phosphatase non-receptor type 1 A Protein-tyrosine phosphatase 1B,PTP-1B
ec: 3.1.3.48
fragment: catalytic domain
mutation: C32S, C92V
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:469008)
gene: PTPN1, PTP1B
expression_system_strain: BL21(DE3)
expression_system_vector_type: plasmid
expression_system_plasmid: pET24b
Authors : Keedy, D.A., Hill, Z.B., Biel, J.T., Kang, E., Rettenmaier, T.J., Brandao-Neto, J., von Delft, F., Wells, J.A., Fraser, J.S.
Keywords : PanDDA, SGC - Diamond I04-1 fragment screening, protein tyrosine phosphatase, PTP, protein tyrosine phosphatase 1B, PTP1B, enzyme, allostery, multiconformer, HYDROLASE
Exp. method : X-RAY DIFFRACTION ( 1.7710 Å )
Citation :

An expanded allosteric network in PTP1B by multitemperature crystallography, fragment screening, and covalent tethering.

Keedy, D.A.,Hill, Z.B.,Biel, J.T.  et al.
(2018)  Elife  7

PubMed: 29877794
DOI: 10.7554/eLife.36307

Chain : A
UniProt : P18031 (PTN1_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate 3.1.3.48 PROSITE- ProRule:PRU10044
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