› 4na8

X-ray diffraction
2.3Å resolution

Factor XIa in complex with the inhibitor 5-aminocarbonyl-2-[3-[(2s,4r)-6-carbamimidoyl-4-methyl-4-phenyl-2,3-dihydro-1h-quinolin-2-yl]phenyl]benzoic acid

Released:
DOI: 10.2210/pdb4na8/pdb
PDB entry 4na8 coloured by chain, front view.
PDB entry 4na8 coloured by chain, side view.
PDB entry 4na8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Tetrahydroquinoline derivatives as potent and selective factor XIa inhibitors.
Quan ML, Wong PC, Wang C, Woerner F, Smallheer JM, Barbera FA, Bozarth JM, Brown RL, Harpel MR, Luettgen JM, Morin PE, Peterson T, Ramamurthy V, Rendina AR, Rossi KA, Watson CA, Wei A, Zhang G, Seiffert D, Wexler RR
J Med Chem 57 955-69 (2014)
PMID: 24405333

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137278 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Coagulation factor XIa light chain Chain: A
Molecule details ›
Chain: A
Length: 244 amino acids
Theoretical weight: 27.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P03951 (Residues: 388-625; Coverage: 39%)
Gene name: F11
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

3 bound ligands:
Ligand 1T6 1 x 1T6
Ligand SO4 1 x SO4
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P3221
Unit cell:
a: 79.05Å b: 79.05Å c: 106.91Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.23 0.23 0.271
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Factors XI and XII as Targets for New Anticoagulants.
Weitz et al. (2017)
7 more

1 mention without citation

Homology modeling of TMPRSS2 yields candidate drugs that may inhibit entry of SARS-CoV-2 into human cells.
Rensi et al. (2020)