3gm1

X-ray diffraction
2.95Å resolution

Crystal Structure of the Focal Adhesion Targeting (FAT) Domain of Pyk2 in Complex with Paxillin LD4 Motif-Derived Peptides

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structures of free and ligand-bound focal adhesion targeting domain of Pyk2.
Biochem. Biophys. Res. Commun. 383 347-52 (2009)
PMID: 19358827

Function and Biology Details

Reaction catalysed:
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
Non-polymer only trimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein-tyrosine kinase 2-beta Chains: A, B
Molecule details ›
Chains: A, B
Length: 153 amino acids
Theoretical weight: 16.69 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q14289 (Residues: 861-1009; Coverage: 15%)
Gene names: FAK2, PTK2B, PYK2, RAFTK
Sequence domains: Focal adhesion targeting region
Structure domains: Nucleotidyltransferases domain 2
Paxillin Chains: C, D, E, F
Molecule details ›
Chains: C, D, E, F
Length: 13 amino acids
Theoretical weight: 1.44 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P49023 (Residues: 262-274; Coverage: 2%)
Gene name: PXN

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P41212
Unit cell:
a: 73.774Å b: 73.774Å c: 156.925Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.233 0.29
Expression systems:
  • Escherichia coli
  • Not provided