› 5lpx

X-ray diffraction
1.9Å resolution

Crystal structure of PKC phosphorylation-mimicking mutant (S26E) Annexin A2

Released:
DOI: 10.2210/pdb5lpx/pdb
PDB entry 5lpx coloured by chain, front view.
PDB entry 5lpx coloured by chain, side view.
PDB entry 5lpx coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Regulation of the Equilibrium between Closed and Open Conformations of Annexin A2 by N-Terminal Phosphorylation and S100A4-Binding.
Ecsédi P, Kiss B, Gógl G, Radnai L, Buday L, Koprivanacz K, Liliom K, Leveles I, Vértessy B, Jeszenői N, Hetényi C, Schlosser G, Katona G, Nyitray L
Structure 25 1195-1207.e5 (2017)
PMID: 28669632

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139552 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Annexin A2 Chain: A
Molecule details ›
Chain: A
Length: 339 amino acids
Theoretical weight: 38.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P07355 (Residues: 2-339; Coverage: 100%)
Gene names: ANX2, ANX2L4, ANXA2, CAL1H, LPC2D
Sequence domains: Annexin
Structure domains: Annexin

Ligands and Environments

2 bound ligands:
Ligand CA 5 x CA
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Unit cell:
a: 54.95Å b: 58.76Å c: 182.09Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.147 0.146 0.182
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Advances in cancer treatment: a new therapeutic target, Annexin A2.
Li et al. (2021)
6 more