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Chlorine in PDB 1v2k: Factor Xa Specific Inhibitor in Complex with Bovine Trypsin Variant X(Triple.Glu)Bt.D2

Enzymatic activity of Factor Xa Specific Inhibitor in Complex with Bovine Trypsin Variant X(Triple.Glu)Bt.D2

All present enzymatic activity of Factor Xa Specific Inhibitor in Complex with Bovine Trypsin Variant X(Triple.Glu)Bt.D2:
3.4.21.4;

Protein crystallography data

The structure of Factor Xa Specific Inhibitor in Complex with Bovine Trypsin Variant X(Triple.Glu)Bt.D2, PDB code: 1v2k was solved by D.Rauh, G.Klebe, M.T.Stubbs, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.00
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 54.750, 54.750, 144.070, 90.00, 90.00, 120.00
R / Rfree (%) 19.2 / 22.3

Other elements in 1v2k:

The structure of Factor Xa Specific Inhibitor in Complex with Bovine Trypsin Variant X(Triple.Glu)Bt.D2 also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Factor Xa Specific Inhibitor in Complex with Bovine Trypsin Variant X(Triple.Glu)Bt.D2 (pdb code 1v2k). 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 Factor Xa Specific Inhibitor in Complex with Bovine Trypsin Variant X(Triple.Glu)Bt.D2, PDB code: 1v2k:

Chlorine binding site 1 out of 1 in 1v2k

Go back to Chlorine Binding Sites List in 1v2k
Chlorine binding site 1 out of 1 in the Factor Xa Specific Inhibitor in Complex with Bovine Trypsin Variant X(Triple.Glu)Bt.D2


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Factor Xa Specific Inhibitor in Complex with Bovine Trypsin Variant X(Triple.Glu)Bt.D2 within 5.0Å range:
probe atom residue distance (Å) B Occ
T:Cl1

b:1.0
occ:1.00
 CL32 T:ZEN1 0.0 1.0 1.0
C29 T:ZEN1 1.7 15.6 1.0
C28 T:ZEN1 2.7 18.1 1.0
C30 T:ZEN1 2.8 18.2 1.0
O T:HOH605 2.9 79.6 1.0
CZ T:TYR228 3.4 25.6 1.0
OH T:TYR228 3.5 25.8 1.0
O T:VAL227 3.6 20.7 1.0
CE1 T:TYR228 3.6 26.3 1.0
O T:TRP215 3.6 23.2 1.0
CA T:GLY226 3.7 24.6 1.0
N T:VAL227 3.7 22.4 1.0
CG1 T:VAL213 3.7 16.1 1.0
CB T:ALA190 3.8 21.9 1.0
CE2 T:TYR228 3.8 26.3 1.0
C27 T:ZEN1 4.0 21.2 1.0
C T:GLY226 4.0 24.0 1.0
C31 T:ZEN1 4.1 20.4 1.0
CD1 T:TYR228 4.2 23.1 1.0
C T:TRP215 4.3 23.8 1.0
N T:SER214 4.3 20.3 1.0
N T:TRP215 4.3 20.3 1.0
C T:VAL227 4.3 20.6 1.0
CD2 T:TYR228 4.4 22.5 1.0
OD2 T:ASP189 4.5 22.7 1.0
CA T:VAL213 4.5 19.6 1.0
C26 T:ZEN1 4.6 22.0 1.0
CG T:TYR228 4.6 23.8 1.0
CA T:VAL227 4.7 20.1 1.0
CB T:VAL213 4.7 19.7 1.0
CA T:TRP215 4.7 22.1 1.0
O T:HOH601 4.7 22.0 1.0
C T:VAL213 4.8 19.9 1.0
C T:SER214 4.9 20.1 1.0
CA T:ALA190 4.9 23.6 1.0
O T:GLY226 5.0 23.4 1.0

Reference:

D.Rauh, G.Klebe, M.T.Stubbs. Understanding Protein-Ligand Interactions: the Price of Protein Flexibility J.Mol.Biol. V. 335 1325 2004.
ISSN: ISSN 0022-2836
PubMed: 14729347
DOI: 10.1016/J.JMB.2003.11.041
Page generated: Thu Jul 10 19:49:18 2025

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