› 4ftg

X-ray diffraction
2.51Å resolution

The crystal structure of an AHNAK peptide in complex with the S100A10/AnxA2 heterotetramer

Released:
DOI: 10.2210/pdb4ftg/pdb
PDB entry 4ftg coloured by chain, front view.
PDB entry 4ftg coloured by chain, side view.
PDB entry 4ftg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of a C-terminal AHNAK peptide in a 1:2:2 complex with S100A10 and an acetylated N-terminal peptide of annexin A2.
Ozorowski G, Milton S, Luecke H
Acta Crystallogr D Biol Crystallogr 69 92-104 (2013)
PMID: 23275167

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139555 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Protein S100-A10 Chains: A, B
Molecule details ›
Chains: A, B
Length: 96 amino acids
Theoretical weight: 11.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P60903 (Residues: 2-97; Coverage: 99%)
Gene names: ANX2LG, CAL1L, CLP11, S100A10
Sequence domains: S-100/ICaBP type calcium binding domain
Structure domains: EF-hand
Annexin A2 Chains: C, D
Molecule details ›
Chains: C, D
Length: 17 amino acids
Theoretical weight: 1.65 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P07355 (Residues: 2-16; Coverage: 4%)
Gene names: ANX2, ANX2L4, ANXA2, CAL1H, LPC2D
Neuroblast differentiation-associated protein AHNAK Chain: E
Molecule details ›
Chain: E
Length: 22 amino acids
Theoretical weight: 2.34 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q09666 (Residues: 5654-5673; Coverage: 0%)
Gene names: AHNAK, PM227

Ligands and Environments

1 bound ligand:
Ligand IPA 3 x IPA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.1
Spacegroup: C2
Unit cell:
a: 79.072Å b: 55.216Å c: 63.14Å
α: 90° β: 111.73° γ: 90°
R-values:
R R work R free
0.185 0.181 0.251
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

7 review citations

Annexin A2 complexes with S100 proteins: structure, function and pharmacological manipulation.
Liu et al. (2015)
6 more

8 mentions without citation

Zooming into the Dark Side of Human Annexin-S100 Complexes: Dynamic Alliance of Flexible Partners.
Weisz et al. (2020)
7 more