› 1pa1

X-ray diffraction
1.6Å resolution

Crystal structure of the C215D mutant of protein tyrosine phosphatase 1B

Released:
DOI: 10.2210/pdb1pa1/pdb
PDB entry 1pa1 coloured by chain, front view.
PDB entry 1pa1 coloured by chain, side view.
PDB entry 1pa1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Functional characterization and crystal structure of the C215D mutant of protein-tyrosine phosphatase-1B.
Romsicki Y, Scapin G, Beaulieu-Audy V, Patel S, Becker JW, Kennedy BP, Asante-Appiah E
J Biol Chem 278 29009-15 (2003)
PMID: 12748196

Function and Biology Details

Reaction catalysed: 
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148259 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine-protein phosphatase non-receptor type 1 Chain: A
Molecule details ›
Chain: A
Length: 310 amino acids
Theoretical weight: 36.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P18031 (Residues: 1-298; Coverage: 69%)
Gene names: PTP1B, PTPN1
Sequence domains: Protein-tyrosine phosphatase
Structure domains: Protein tyrosine phosphatase superfamily

Ligands and Environments

2 bound ligands:
Ligand MG 2 x MG
Ligand CL 6 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P3121
Unit cell:
a: 88.451Å b: 88.451Å c: 104.356Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.186 0.204
Expression system: Escherichia coli BL21(DE3)

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Citations

3 citation in other articles

An inverse substrate orientation for the regioselective acylation of 3',5'-diaminonucleosides catalyzed by Candida antarctica lipase B?
Lavandera et al. (2005)
2 more

4 mentions without citation

New Frontiers in Druggability.
Kozakov et al. (2015)
3 more