› 2qfg

X-ray solution scattering

Solution Structure of the N-terminal SCR-1/5 fragment of Complement Factor H.

Released:
DOI: 10.2210/pdb2qfg/pdb
PDB entry 2qfg coloured by chain, ensemble of 12 models, front view.
PDB entry 2qfg coloured by chain, ensemble of 12 models, side view.
PDB entry 2qfg coloured by chain, ensemble of 12 models, top view.
Source organism: Homo sapiens
Primary publication:
The regulatory SCR-1/5 and cell surface-binding SCR-16/20 fragments of factor H reveal partially folded-back solution structures and different self-associative properties.
Okemefuna AI, Gilbert HE, Griggs KM, Ormsby RJ, Gordon DL, Perkins SJ
J Mol Biol 375 80-101 (2008)
PMID: 18005991

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-140213 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Complement factor H Chain: A
Molecule details ›
Chain: A
Length: 312 amino acids
Theoretical weight: 35.43 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P08603 (Residues: 19-322; Coverage: 25%)
Gene names: CFH, HF, HF1, HF2
Sequence domains: Sushi repeat (SCR repeat)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Expression system: Komagataella pastoris

Quick links

Citations

6 review citations

Complement control protein factor H: the good, the bad, and the inadequate.
Ferreira et al. (2010)
5 more

3 mentions without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)
2 more