› 1ssu

Solution NMR

Structural and biochemical evidence for disulfide bond heterogeneity in active forms of the somatomedin B domain of human vitronectin

Released:
DOI: 10.2210/pdb1ssu/pdb
PDB entry 1ssu coloured by chain, ensemble of 20 models, front view.
PDB entry 1ssu coloured by chain, ensemble of 20 models, side view.
PDB entry 1ssu coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Disulfide bonding arrangements in active forms of the somatomedin B domain of human vitronectin.
Kamikubo Y, De Guzman R, Kroon G, Curriden S, Neels JG, Churchill MJ, Dawson P, Ołdziej S, Jagielska A, Scheraga HA, Loskutoff DJ, Dyson HJ
Biochemistry 43 6519-34 (2004)
PMID: 15157085

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137317 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Somatomedin-B Chain: A
Molecule details ›
Chain: A
Length: 51 amino acids
Theoretical weight: 5.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04004 (Residues: 20-70; Coverage: 11%)
Gene name: VTN
Sequence domains: Somatomedin B domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics in DYANA followed by simulated annealing and energy minimization in AMBER
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Cellular function and molecular structure of ecto-nucleotidases.
Zimmermann et al. (2012)
3 more

3 mentions without citation

Solution structure of recombinant somatomedin B domain from vitronectin produced in Pichia pastoris.
Kjaergaard et al. (2007)
2 more