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Magnesium 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:

Bromine (Br) 1 atom
Chlorine (Cl) 2 atoms
Calcium (Ca) 4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium 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 Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Fviia in Complex with A Benzamidine-Based Inhibitor, PDB code: 8qod:

Magnesium binding site 1 out of 1 in 8qod

Go back to Magnesium Binding Sites List in 8qod
Magnesium 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 Magnesium with other atoms in the Mg 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
A:Mg202

b:33.8
occ:0.74
 OE11 A:CGU16 2.0 45.1 1.0
OE21 A:CGU16 2.0 45.3 1.0
OE12 A:CGU26 2.1 36.6 1.0
OE22 A:CGU26 2.1 35.9 1.0
O A:HOH331 2.4 49.0 1.0
CD1 A:CGU16 2.8 45.4 1.0
CD2 A:CGU16 2.8 45.5 1.0
CD1 A:CGU26 3.1 36.4 1.0
CG A:CGU16 3.2 46.0 1.0
CD2 A:CGU26 3.2 36.1 1.0
CG A:CGU26 3.6 35.8 1.0
CB A:CGU16 3.7 47.4 1.0
O A:HOH388 4.0 37.8 1.0
O A:HOH306 4.0 65.9 1.0
OE22 A:CGU16 4.0 45.2 1.0
OE12 A:CGU16 4.0 45.4 1.0
OE12 A:CGU7 4.2 48.0 1.0
OE11 A:CGU7 4.2 48.5 1.0
OE21 A:CGU26 4.3 36.3 1.0
OE11 A:CGU26 4.3 37.0 1.0
CB A:CGU26 4.4 34.4 1.0
O A:HOH343 4.5 39.2 1.0
O A:HOH437 4.6 69.5 1.0
CD1 A:CGU7 4.7 48.1 1.0
CA A:CGU16 4.8 49.0 1.0
O A:HOH315 5.0 50.7 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 21:59:10 2024

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