PDBsum entry 2fda

Hydrolase

PDB id: 2fda

Contents

Protein chain

237 a.a. *

Ligands

BCT ×2

SO4

682

Waters ×255

* Residue conservation analysis

PDB id:

2fda

Name:

Hydrolase

Title:

Crystal structure of the catalytic domain of human coagulation factor xia in complex with alpha-ketothiazole arginine derived ligand

Structure:

Coagulation factor xi. Chain: a. Fragment: light chain, catalytic domain, residues 388-625. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: f11. Expressed in: pichia pastoris. Expression_system_taxid: 4922.

Resolution:

2.00Å R-factor: 0.186 R-free: 0.213

Authors:

L.Jin,P.Pandey,R.E.Babine,D.T.Weaver,S.S.Abdel-Meguid,J.E.Strickler

Key ref:

H.Deng et al. (2006). Synthesis, SAR exploration, and X-ray crystal structures of factor XIa inhibitors containing an alpha-ketothiazole arginine. Bioorg Med Chem Lett, 16, 3049-3054. PubMed id: 16524727 DOI: 10.1016/j.bmcl.2006.02.052

Date:

13-Dec-05 Release date: 18-Apr-06

Protein chain

P03951  (FA11_HUMAN) -  Coagulation factor XI from Homo sapiens

Seq: 625 a.a.

Struc: 237 a.a.*

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.4.21.27 - coagulation factor XIa.
• Reaction: Selective cleavage of Arg-|-Ala and Arg-|-Val bonds in factor IX to form factor IXa.

DOI no: 10.1016/j.bmcl.2006.02.052

Bioorg Med Chem Lett 16:3049-3054 (2006)

PubMed id: 16524727

Synthesis, SAR exploration, and X-ray crystal structures of factor XIa inhibitors containing an alpha-ketothiazole arginine.

H.Deng, T.D.Bannister, L.Jin, R.E.Babine, J.Quinn, P.Nagafuji, C.A.Celatka, J.Lin, T.I.Lazarova, M.J.Rynkiewicz, F.Bibbins, P.Pandey, J.Gorga, H.V.Meyers, S.S.Abdel-Meguid, J.E.Strickler.

ABSTRACT

Using an alpha-ketothiazole arginine moiety as a key recognition element, a series of small peptidomimetic molecules was designed and synthesized, and their co-crystal structures with factor XIa were studied in an effort to develop smaller, less peptidic inhibitors as antithrombotic agents.