PDBe 1zpz

X-ray diffraction
2.5Å resolution

Factor XI catalytic domain complexed with N-((R)-1-(4-bromophenyl)ethyl)urea-Asn-Val-Arg-alpha-ketothiazole

Released:
Source organism: Homo sapiens
Entry authors: Lin J, Deng H, Jin L, Prandey P, Rynkiewicz MJ, Bibbins F, Cantin S, Quinn J, Magee S, Gorga J

Function and Biology Details

Reaction catalysed:
Selective cleavage of Arg-|-Ala and Arg-|-Val bonds in factor IX to form factor IXa.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Coagulation factor XIa light chain Chain: A
Molecule details ›
Chain: A
Length: 238 amino acids
Theoretical weight: 26.8 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: NEW P03951 (Residues: 388-625; Coverage: 39%)
Gene name: F11
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P32
Unit cell:
a: 41.937Å b: 41.937Å c: 103.872Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.221 0.221 0.272
Expression system: Komagataella pastoris