› 5tca

X-ray diffraction
3.15Å resolution

Complement Factor D inhibited with JH3

Released:
DOI: 10.2210/pdb5tca/pdb
PDB entry 5tca coloured by chain, front view.
PDB entry 5tca coloured by chain, side view.
PDB entry 5tca coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Buried Hydrogen Bond Interactions Contribute to the High Potency of Complement Factor D Inhibitors.
Yang CY, Phillips JG, Stuckey JA, Bai L, Sun H, Delproposto J, Brown WC, Chinnaswamy K
ACS Med Chem Lett 7 1092-1096 (2016)
PMID: 27994744

Function and Biology Details

Reaction catalysed: 
Selective cleavage of Arg-|-Lys bond in complement factor B when in complex with complement subcomponent C3b or with cobra venom factor.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133224 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Complement factor D Chains: A, B, C, D, E, F, G
Molecule details ›
Chains: A, B, C, D, E, F, G
Length: 228 amino acids
Theoretical weight: 24.44 KDa
Source organism: Homo sapiens
Expression system: unidentified baculovirus
UniProt:
  • Canonical: P00746 (Residues: 26-253; Coverage: 98%)
Gene names: CFD, DF, PFD
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:
Ligand J55 9 x J55
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: C2221
Unit cell:
a: 99.361Å b: 143.654Å c: 347.592Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.225 0.264
Expression system: unidentified baculovirus

Quick links

Citations

3 review citations

Surface loops of trypsin-like serine proteases as determinants of function.
Goettig et al. (2019)
2 more

1 mention without citation

Isotope-Labeled RNA Building Blocks for NMR Structure and Dynamics Studies.
Olenginski et al. (2021)