› 3hqa

X-ray diffraction
2.59Å resolution

Crystal structure of human desarg-C5A

Released:
DOI: 10.2210/pdb3hqa/pdb
PDB entry 3hqa coloured by chain, front view.
PDB entry 3hqa coloured by chain, side view.
PDB entry 3hqa coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of human desArg-C5a.
Cook WJ, Galakatos N, Boyar WC, Walter RL, Ealick SE
Acta Crystallogr D Biol Crystallogr 66 190-7 (2010)
PMID: 20124699

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-133860 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
C5a anaphylatoxin Chains: A, B
Molecule details ›
Chains: A, B
Length: 73 amino acids
Theoretical weight: 8.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P01031 (Residues: 679-750; Coverage: 4%)
Gene names: C5, CPAMD4
Sequence domains: Anaphylotoxin-like domain
Structure domains: Anaphylotoxins (complement system)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P41212
Unit cell:
a: 50.61Å b: 50.61Å c: 117.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.213 0.253
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Complement System Part I - Molecular Mechanisms of Activation and Regulation.
Merle et al. (2015)
4 more

10 mentions without citation

Marine natural product peptides with therapeutic potential: Chemistry, biosynthesis, and pharmacology.
Gogineni et al. (2018)
9 more