› 2vzc

X-ray diffraction
1.05Å resolution

Crystal structure of the C-terminal calponin homology domain of alpha parvin

Released:
DOI: 10.2210/pdb2vzc/pdb
PDB entry 2vzc coloured by chain, front view.
PDB entry 2vzc coloured by chain, side view.
PDB entry 2vzc coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural analysis of the interactions between paxillin LD motifs and alpha-parvin.
Lorenz S, Vakonakis I, Lowe ED, Campbell ID, Noble ME, Hoellerer MK
Structure 16 1521-31 (2008)
PMID: 18940607

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192632 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-parvin Chains: A, B
Molecule details ›
Chains: A, B
Length: 131 amino acids
Theoretical weight: 15.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9NVD7 (Residues: 242-372; Coverage: 35%)
Gene names: MXRA2, PARVA
Sequence domains: Calponin homology (CH) domain
Structure domains: Calponin-like domain

Ligands and Environments

4 bound ligands:
Ligand TRS 1 x TRS
Ligand GOL 1 x GOL
Ligand MRD 1 x MRD
Ligand MPD 1 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P21
Unit cell:
a: 44.144Å b: 71.197Å c: 47.146Å
α: 90° β: 99.88° γ: 90°
R-values:
R R work R free
0.144 0.143 0.159
Expression system: Escherichia coli BL21

Quick links

Citations

5 review citations

The ILK/PINCH/parvin complex: the kinase is dead, long live the pseudokinase!
Wickström et al. (2010)
4 more

4 mentions without citation

TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts.
Shen et al. (2009)
3 more