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Chlorine in PDB 1nfy: Crystal Structure of Human Coagulation Factor Xa Complexed with RPR200095

Enzymatic activity of Crystal Structure of Human Coagulation Factor Xa Complexed with RPR200095

All present enzymatic activity of Crystal Structure of Human Coagulation Factor Xa Complexed with RPR200095:
3.4.21.6;

Protein crystallography data

The structure of Crystal Structure of Human Coagulation Factor Xa Complexed with RPR200095, PDB code: 1nfy was solved by S.Maignan, J.P.Guilloteau, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 55.783, 71.828, 79.045, 90.00, 90.00, 90.00
R / Rfree (%) 20.3 / n/a

Other elements in 1nfy:

The structure of Crystal Structure of Human Coagulation Factor Xa Complexed with RPR200095 also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Human Coagulation Factor Xa Complexed with RPR200095 (pdb code 1nfy). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Human Coagulation Factor Xa Complexed with RPR200095, PDB code: 1nfy:

Chlorine binding site 1 out of 1 in 1nfy

Go back to Chlorine Binding Sites List in 1nfy
Chlorine binding site 1 out of 1 in the Crystal Structure of Human Coagulation Factor Xa Complexed with RPR200095


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Human Coagulation Factor Xa Complexed with RPR200095 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl301

b:16.9
occ:1.00
 CL A:RTR301 0.0 16.9 1.0
C14 A:RTR301 1.7 16.9 1.0
C15 A:RTR301 2.7 16.7 1.0
C10 A:RTR301 2.7 16.8 1.0
CZ A:TYR228 3.4 16.4 1.0
O A:ILE227 3.7 14.2 1.0
OH A:TYR228 3.7 13.3 1.0
CE2 A:TYR228 3.7 14.2 1.0
CE1 A:TYR228 3.7 15.6 1.0
N A:ILE227 3.7 16.8 1.0
O A:TRP215 3.8 19.2 1.0
CA A:GLY226 3.8 19.9 1.0
CB A:ALA190 3.8 15.1 1.0
CG1 A:VAL213 3.8 15.1 1.0
C A:GLY226 3.9 16.5 1.0
C5 A:RTR301 4.0 19.0 1.0
C11 A:RTR301 4.0 15.5 1.0
CD2 A:TYR228 4.2 11.8 1.0
C A:ILE227 4.2 15.2 1.0
CD1 A:TYR228 4.2 13.4 1.0
N A:SER214 4.3 17.8 1.0
O A:HOH324 4.3 15.8 1.0
CG A:TYR228 4.4 13.6 1.0
CA A:VAL213 4.5 16.9 1.0
N A:TRP215 4.5 17.8 1.0
C6 A:RTR301 4.5 18.1 1.0
C A:TRP215 4.5 19.6 1.0
CA A:ILE227 4.6 14.4 1.0
OD1 A:ASP189 4.6 22.8 1.0
CB A:VAL213 4.6 16.0 1.0
O A:GLY226 4.7 14.4 1.0
C A:VAL213 4.8 18.2 1.0
CG2 A:VAL213 4.9 10.9 1.0
N A:TYR228 5.0 15.2 1.0
CA A:TRP215 5.0 19.2 1.0

Reference:

S.Maignan, J.P.Guilloteau, Y.M.Choi-Sledeski, M.R.Becker, W.R.Ewing, H.W.Pauls, A.P.Spada, V.Mikol. Molecular Structures of Human Factor Xa Complexed with Ketopiperazine Inhibitors: Preference For A Neutral Group in the S1 Pocket. J.Med.Chem. V. 46 685 2003.
ISSN: ISSN 0022-2623
PubMed: 12593649
DOI: 10.1021/JM0203837
Page generated: Thu Jul 10 18:27:10 2025

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