PDBe 1ztl

X-ray diffraction
2.6Å resolution

Crystal Structure of the Catalytic Domain of Coagulation Factor XI in Complex with N-[4-Guanidino-1-(thiazole-2-carbonyl)-butyl]-2-{6-oxo-5-[(quinolin-8-ylmethyl)-amino]-2-m-tolyl-6H-pyrimidin-1-yl}-acetamide

Released:
Source organism: Homo sapiens
Entry authors: Nagafuji P, Jin L, Rynkiewicz M, Quinn J, Bibbins F, Meyers H, Babine R, Strickler JE, Abdel-Meguid SS

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: 26.75 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: 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: I23
Unit cell:
a: 121.965Å b: 121.965Å c: 121.965Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.208 0.237
Expression system: Komagataella pastoris