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Bromine in PDB 8qod: Crystal Structure of Fviia in Complex with A Benzamidine-Based Inhibitor

Enzymatic activity of Crystal Structure of Fviia in Complex with A Benzamidine-Based Inhibitor

All present enzymatic activity of Crystal Structure of Fviia in Complex with A Benzamidine-Based Inhibitor:
3.4.21.21;

Protein crystallography data

The structure of Crystal Structure of Fviia in Complex with A Benzamidine-Based Inhibitor, PDB code: 8qod was solved by H.A.Schreuder, A.Liesum, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 22.88 / 1.57
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 69.811, 81.51, 125.498, 90, 90, 90
R / Rfree (%) 18.2 / 21.4

Other elements in 8qod:

The structure of Crystal Structure of Fviia in Complex with A Benzamidine-Based Inhibitor also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms
Magnesium (Mg) 1 atom
Calcium (Ca) 4 atoms

Bromine Binding Sites:

The binding sites of Bromine atom in the Crystal Structure of Fviia in Complex with A Benzamidine-Based Inhibitor (pdb code 8qod). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Crystal Structure of Fviia in Complex with A Benzamidine-Based Inhibitor, PDB code: 8qod:

Bromine binding site 1 out of 1 in 8qod

Go back to Bromine Binding Sites List in 8qod
Bromine binding site 1 out of 1 in the Crystal Structure of Fviia in Complex with A Benzamidine-Based Inhibitor


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of Fviia in Complex with A Benzamidine-Based Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Br301

b:24.9
occ:0.82
 BR16 B:WIZ301 0.0 24.9 0.8
C11 B:WIZ301 1.9 22.0 0.8
C12 B:WIZ301 2.8 20.2 0.8
C10 B:WIZ301 2.8 20.9 0.8
O15 B:WIZ301 3.0 21.6 0.8
O B:HOH645 3.8 36.9 1.0
CE3 B:TRP215 3.9 14.6 1.0
O B:HOH737 4.0 62.6 1.0
O B:GLY216 4.0 20.4 1.0
O B:HOH792 4.1 48.8 1.0
C9 B:WIZ301 4.1 20.1 0.8
C13 B:WIZ301 4.1 19.2 0.8
O B:HOH676 4.2 46.9 1.0
CB B:TRP215 4.2 13.7 1.0
C20 B:WIZ301 4.3 21.3 0.8
CG B:PRO170I 4.4 25.2 1.0
CG2 B:THR99 4.5 16.5 1.0
CD2 B:TRP215 4.5 14.0 1.0
O31 B:WIZ301 4.6 18.9 0.8
C14 B:WIZ301 4.6 19.6 0.8
CZ3 B:TRP215 4.7 15.4 1.0
CG B:TRP215 4.7 13.9 1.0
N B:GLY216 4.8 16.7 1.0
C19 B:WIZ301 4.9 20.7 0.8
O B:HOH718 4.9 70.5 1.0
C B:GLY216 5.0 19.6 1.0

Reference:

L.Tesmer, H.Hans Matter, O.Klingler, M.Schudok, G.Hessler, A.R.Mehdipour, S.Guessregen, G.Hummer, H.A.Schreuder. Crystallography and Molecular Simulations Capture S1 Pocket Collapse in Allosteric Regulation of Factor Viia and Other Serine Proteases. To Be Published.
Page generated: Thu Oct 31 16:50:51 2024

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