3aae

X-ray diffraction
3.3Å resolution

Crystal structure of Actin capping protein in complex with CARMIL fragment

Released:
Source organisms:
Entry authors: Takeda S, Minakata S, Narita A, Kitazawa M, Yamakuni T, Maeda Y, Nitanai Y

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-146480 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
F-actin-capping protein subunit alpha-1 Chains: A, C, E, G, I
Molecule details ›
Chains: A, C, E, G, I
Length: 286 amino acids
Theoretical weight: 33 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
UniProt:
  • Canonical: P13127 (Residues: 1-286; Coverage: 100%)
Gene name: CAPZA1
Sequence domains: F-actin capping protein alpha subunit
Structure domains:
F-actin-capping protein subunit beta isoforms 1 and 2 Chains: B, D, F, H, J
Molecule details ›
Chains: B, D, F, H, J
Length: 277 amino acids
Theoretical weight: 31.4 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
UniProt:
  • Canonical: P14315 (Residues: 1-277; Coverage: 100%)
Gene name: CAPZB
Sequence domains: F-actin capping protein, beta subunit
Structure domains:
F-actin-uncapping protein LRRC16A Chains: V, W, X, Y, Z
Molecule details ›
Chains: V, W, X, Y, Z
Length: 37 amino acids
Theoretical weight: 4.17 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6EDY6 (Residues: 971-1002; Coverage: 2%)
Gene names: Carmil, Carmil1, Lrrc16, Lrrc16a

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: C2
Unit cell:
a: 231.153Å b: 104.358Å c: 186.633Å
α: 90° β: 119.09° γ: 90°
R-values:
R R work R free
0.245 0.243 0.271
Expression system: Escherichia coli