› 1ury

X-ray diffraction
2.4Å resolution

cytoglobin cavities

Released:
DOI: 10.2210/pdb1ury/pdb
PDB entry 1ury coloured by chain, front view.
PDB entry 1ury coloured by chain, side view.
PDB entry 1ury coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Mapping protein matrix cavities in human cytoglobin through Xe atom binding.
de Sanctis D, Dewilde S, Pesce A, Moens L, Ascenzi P, Hankeln T, Burmester T, Bolognesi M
Biochem Biophys Res Commun 316 1217-21 (2004)
PMID: 15044115

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186754 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytoglobin Chains: A, B
Molecule details ›
Chains: A, B
Length: 190 amino acids
Theoretical weight: 21.4 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8WWM9 (Residues: 1-190; Coverage: 100%)
Gene names: CYGB, STAP
Sequence domains: Globin
Structure domains: Globins

Ligands and Environments

3 bound ligands:
Ligand HEM 2 x HEM
Ligand XE 7 x XE
Ligand FC6 2 x FC6
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF
Spacegroup: P212121
Unit cell:
a: 47.848Å b: 70.524Å c: 98.728Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.197 0.254
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Functional aspects of protein flexibility.
Teilum et al. (2009)
4 more

2 mentions without citation

CO rebinding kinetics and molecular dynamics simulations highlight dynamic regulation of internal cavities in human cytoglobin.
Gabba et al. (2013)
1 more