› 1xwe

Solution NMR

NMR Structure of C345C (NTR) domain of C5 of complement

Released:
DOI: 10.2210/pdb1xwe/pdb
PDB entry 1xwe coloured by chain, ensemble of 40 models, front view.
PDB entry 1xwe coloured by chain, ensemble of 40 models, side view.
PDB entry 1xwe coloured by chain, ensemble of 40 models, top view.
Source organism: Homo sapiens
Primary publication:
Functional insights from the structure of the multifunctional C345C domain of C5 of complement.
Bramham J, Thai CT, Soares DC, Uhrín D, Ogata RT, Barlow PN
J Biol Chem 280 10636-45 (2005)
PMID: 15598652

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-133860 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Complement C5 alpha' chain Chain: A
Molecule details ›
Chain: A
Length: 151 amino acids
Theoretical weight: 17.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01031 (Residues: 1530-1676; Coverage: 9%)
Gene names: C5, CPAMD4
Sequence domains: UNC-6/NTR/C345C module
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated anneailing, restrained molecular dynamics
Expression system: Escherichia coli

Quick links

Citations

4 review citations

The tissue inhibitors of metalloproteinases (TIMPs): an ancient family with structural and functional diversity.
Brew et al. (2010)
3 more

5 mentions without citation

Constraint methods that accelerate free-energy simulations of biomolecules.
Perez et al. (2015)
4 more