› 2a55

Solution NMR

Solution structure of the two N-terminal CCP modules of C4b-binding protein (C4BP) alpha-chain.

Released:
DOI: 10.2210/pdb2a55/pdb
PDB entry 2a55 coloured by chain, ensemble of 40 models, front view.
PDB entry 2a55 coloured by chain, ensemble of 40 models, side view.
PDB entry 2a55 coloured by chain, ensemble of 40 models, top view.
Source organism: Homo sapiens
Primary publication:
Human C4b-binding protein, structural basis for interaction with streptococcal M protein, a major bacterial virulence factor.
Jenkins HT, Mark L, Ball G, Persson J, Lindahl G, Uhrin D, Blom AM, Barlow PN
J Biol Chem 281 3690-7 (2006)
PMID: 16330538

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137311 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
C4b-binding protein alpha chain Chain: A
Molecule details ›
Chain: A
Length: 133 amino acids
Theoretical weight: 15.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04003 (Residues: 49-172; Coverage: 23%)
Gene names: C4BP, C4BPA
Sequence domains: Sushi repeat (SCR repeat)
Structure domains: Complement Module, domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: molecular dynamics simulated annealing
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Complement driven by conformational changes.
Gros et al. (2008)
12 more

3 mentions without citation

Structure of the N-terminal region of complement factor H and conformational implications of disease-linked sequence variations.
Hocking et al. (2008)
2 more