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Sodium in PDB 3bv9: Structure of Thrombin Bound to the Inhibitor FM19

Enzymatic activity of Structure of Thrombin Bound to the Inhibitor FM19

All present enzymatic activity of Structure of Thrombin Bound to the Inhibitor FM19:
3.4.21.5;

Protein crystallography data

The structure of Structure of Thrombin Bound to the Inhibitor FM19, PDB code: 3bv9 was solved by M.T.Nieman, F.Burke, M.Warnock, Y.Zhou, J.Sweigert, A.Chen, D.Ricketts, B.R.Lucchesi, Z.Chen, E.Di Cera, J.Hilfinger, H.I.Mosberg, A.H.Schmaier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.03 / 1.80
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 80.907, 80.907, 183.718, 90.00, 90.00, 120.00
R / Rfree (%) 19 / 23.9

Other elements in 3bv9:

The structure of Structure of Thrombin Bound to the Inhibitor FM19 also contains other interesting chemical elements:

Iodine (I) 3 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Structure of Thrombin Bound to the Inhibitor FM19 (pdb code 3bv9). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Structure of Thrombin Bound to the Inhibitor FM19, PDB code: 3bv9:

Sodium binding site 1 out of 1 in 3bv9

Go back to Sodium Binding Sites List in 3bv9
Sodium binding site 1 out of 1 in the Structure of Thrombin Bound to the Inhibitor FM19


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of Thrombin Bound to the Inhibitor FM19 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na307

b:22.5
occ:1.00
O B:HOH336 2.3 21.0 1.0
O B:HOH362 2.3 18.9 1.0
O B:HOH376 2.4 27.8 1.0
O B:LYS224 2.4 23.3 1.0
O B:ARG221A 2.5 20.9 1.0
O B:HOH331 2.5 22.6 1.0
C B:LYS224 3.5 19.1 1.0
C B:ARG221A 3.5 24.3 1.0
N B:LYS224 3.8 21.8 1.0
O B:TYR184A 4.0 16.6 1.0
O B:HOH343 4.0 22.5 1.0
O B:HOH345 4.0 24.2 1.0
N B:ARG221A 4.1 21.1 1.0
O B:HOH340 4.1 20.4 1.0
C B:ASP221 4.1 17.8 1.0
CA B:LYS224 4.2 21.0 1.0
N B:GLY223 4.2 25.4 1.0
CA B:ASP222 4.3 29.5 1.0
N B:ASP222 4.3 22.5 1.0
CA B:ASP221 4.4 17.0 1.0
O B:ASP221 4.4 20.9 1.0
CA B:ARG221A 4.5 22.3 1.0
C B:ASP222 4.5 26.0 1.0
N B:TYR225 4.5 18.1 1.0
CB B:LYS224 4.6 23.9 1.0
OD1 B:ASP221 4.7 24.9 1.0
O B:HOH382 4.7 28.1 1.0
CA B:TYR225 4.8 20.8 1.0
C B:GLY223 4.8 29.9 1.0
CD1 B:TYR225 4.9 18.7 1.0

Reference:

M.T.Nieman, F.Burke, M.Warnock, Y.Zhou, J.Sweigart, A.Chen, D.Ricketts, B.R.Lucchesi, Z.Chen, E.Di Cera, J.Hilfinger, J.S.Kim, H.I.Mosberg, A.H.Schmaier. Thrombostatin Fm Compounds: Direct Thrombin Inhibitors - Mechanism of Action in Vitro and in Vivo. J.Thromb.Haemost. V. 6 837 2008.
ISSN: ISSN 1538-7933
PubMed: 18315550
DOI: 10.1111/J.1538-7836.2008.02937.X
Page generated: Mon Oct 7 06:06:38 2024

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