› 1bhd

X-ray diffraction
2Å resolution

SECOND CALPONIN HOMOLOGY DOMAIN FROM UTROPHIN

Released:
DOI: 10.2210/pdb1bhd/pdb
PDB entry 1bhd coloured by chain, front view.
PDB entry 1bhd coloured by chain, side view.
PDB entry 1bhd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The 2.0 A structure of the second calponin homology domain from the actin-binding region of the dystrophin homologue utrophin.
Keep NH, Norwood FL, Moores CA, Winder SJ, Kendrick-Jones J
J Mol Biol 285 1257-64 (1999)
PMID: 9887274

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155560 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Utrophin Chains: A, B
Molecule details ›
Chains: A, B
Length: 118 amino acids
Theoretical weight: 13.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P46939 (Residues: 144-261; Coverage: 3%)
Gene names: DMDL, DRP1, UTRN
Sequence domains: Calponin homology (CH) domain
Structure domains: Calponin-like domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.5
Spacegroup: P21
Unit cell:
a: 63.92Å b: 32.21Å c: 65.36Å
α: 90° β: 116.25° γ: 90°
R-values:
R R work R free
0.202 0.185 0.257
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Function and genetics of dystrophin and dystrophin-related proteins in muscle.
Blake et al. (2002)
5 more

2 mentions without citation

The dependence of all-atom statistical potentials on structural training database.
Zhang et al. (2004)
1 more