› 1kxp

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF HUMAN VITAMIN D-BINDING PROTEIN IN COMPLEX WITH SKELETAL ACTIN

Released:
DOI: 10.2210/pdb1kxp/pdb
PDB entry 1kxp coloured by chain, front view.
PDB entry 1kxp coloured by chain, side view.
PDB entry 1kxp coloured by chain, top view.
Source organisms:
Primary publication:
Crystal structures of the vitamin D-binding protein and its complex with actin: structural basis of the actin-scavenger system.
Otterbein LR, Cosio C, Graceffa P, Dominguez R
Proc Natl Acad Sci U S A 99 8003-8 (2002)
PMID: 12048248

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136196 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Actin, alpha skeletal muscle Chain: A
Molecule details ›
Chain: A
Length: 375 amino acids
Theoretical weight: 41.86 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P68135 (Residues: 3-377; Coverage: 100%)
Gene names: ACTA, ACTA1
Sequence domains: Actin
Structure domains:
Vitamin D-binding protein Chain: D
Molecule details ›
Chain: D
Length: 458 amino acids
Theoretical weight: 51.31 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P02774 (Residues: 17-474; Coverage: 100%)
Gene name: GC
Sequence domains:
Structure domains: Serum Albumin; Chain A, Domain 1

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand ATP 1 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P212121
Unit cell:
a: 80.758Å b: 87.364Å c: 162.686Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.217 0.236

Quick links

Citations

18 review citations

Radiolytic protein footprinting with mass spectrometry to probe the structure of macromolecular complexes.
Takamoto et al. (2006)
17 more

28 mentions without citation

Protein flexibility in the light of structural alphabets.
Craveur et al. (2015)
27 more