PDBsum entry 2j2u

Hydrolase

PDB id

2j2u

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Contents

			Protein chains

					229 a.a. *


					52 a.a. *

			Ligands

					GSQ

			Waters ×193

* Residue conservation analysis

PDB id:

2j2u

Links
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Name:

Hydrolase

Title:

Crystal structure of a human factor xa inhibitor complex

Structure:

Coagulation factor x heavy chain. Chain: a. Fragment: activated desgla, residues 235-488. Synonym: activated factor xa heavy chain, stuart factor, stuart- prower factor. Other_details: disulphide linked to other chain. Coagulation factor x light chain. Chain: b. Fragment: activated desgla, residues 46-179.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Other_details: purchased from enzym research labs. Isolated from human blood. Human blood

Biol. unit:

Dimer (from PDB file)

Resolution:

1.90Å

R-factor:

0.196

R-free:

0.236

Authors:

S.Senger,M.A.Convery,C.Chan,N.S.Watson

Key ref:

S.Senger et al. (2006). Arylsulfonamides: a study of the relationship between activity and conformational preferences for a series of factor Xa inhibitors. Bioorg Med Chem Lett, 16, 5731-5735. PubMed id: 16982192 DOI: 10.1016/j.bmcl.2006.08.092

Date:

17-Aug-06

Release date:

27-Sep-06

PROCHECK

	Headers

	References

Protein chain

P00742 (FA10_HUMAN) - Coagulation factor X from Homo sapiens

Seq: Struc:					488 a.a. 229 a.a.

Protein chain

P00742 (FA10_HUMAN) - Coagulation factor X from Homo sapiens

Seq: Struc:					488 a.a. 52 a.a.

Key:

PfamA domain

Secondary structure

CATH domain



		Enzyme reactions

Enzyme class:

Chains A, B: E.C.3.4.21.6 - coagulation factor Xa.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Reaction:

Preferential cleavage: Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.

DOI no: 10.1016/j.bmcl.2006.08.092	Bioorg Med Chem Lett 16:5731-5735 (2006)
PubMed id: 16982192

Arylsulfonamides: a study of the relationship between activity and conformational preferences for a series of factor Xa inhibitors.
S.Senger, M.A.Convery, C.Chan, N.S.Watson.

ABSTRACT

Torsional scans of sulfonamide S-C bonds in small model systems of a series of arylsulfonamide factor Xa inhibitors were performed in order to investigate if conformational effects can help to rationalise the observed SAR. Computational results were in good agreement with the experimental data indicating that the sulfonamide conformation plays an important role in determining the activity in this particular series of factor Xa inhibitors.

Literature references that cite this PDB file's key reference

PubMed id

Reference

18266362

R.Abel, T.Young, R.Farid, B.J.Berne, and R.A.Friesner (2008).
Role of the active-site solvent in the thermodynamics of factor Xa ligand binding.

J Am Chem Soc, 130, 2817-2831.

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time.