› 1cwd

X-ray diffraction
2.25Å resolution

HUMAN P56LCK TYROSINE KINASE COMPLEXED WITH PHOSPHOPEPTIDE

Released:
DOI: 10.2210/pdb1cwd/pdb
PDB entry 1cwd coloured by chain, front view.
PDB entry 1cwd coloured by chain, side view.
PDB entry 1cwd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The crystal structures of the SH2 domain of p56lck complexed with two phosphonopeptides suggest a gated peptide binding site.
Mikol V, Baumann G, Keller TH, Manning U, Zurini MG
J Mol Biol 246 344-55 (1995)
PMID: 7532720

Function and Biology Details

Reaction catalysed: 
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138951 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tyrosine-protein kinase Lck Chain: L
Molecule details ›
Chain: L
Length: 98 amino acids
Theoretical weight: 11.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P06239 (Residues: 127-222; Coverage: 19%)
Gene name: LCK
Sequence domains: SH2 domain
Structure domains: SH2 domain
(PHOSPHONOMETHYL)PHENYLALANINE-CONTAINING PEPTIDE PRO-GLU-GLY-ASP-PM3-GLU-GLU-VAL-LEU Chain: P
Molecule details ›
Chain: P
Length: 9 amino acids
Theoretical weight: 1.13 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:
Ligand PM3 1 x PM3

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 44.66Å b: 46.66Å c: 58.298Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.185 not available
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

1 review citation

Searching for specificity in SH domains.
Ladbury et al. (2000)
20 other articles

1 mention without citation

Native, sequential protein folding via anchored N and C protein termini.
Alberti S. (2016)