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Sodium in PDB 2thf: Structure of Human Alpha-Thrombin Y225F Mutant Bound to D-Phe-Pro-Arg- Chloromethylketone

Enzymatic activity of Structure of Human Alpha-Thrombin Y225F Mutant Bound to D-Phe-Pro-Arg- Chloromethylketone

All present enzymatic activity of Structure of Human Alpha-Thrombin Y225F Mutant Bound to D-Phe-Pro-Arg- Chloromethylketone:
3.4.21.5;

Protein crystallography data

The structure of Structure of Human Alpha-Thrombin Y225F Mutant Bound to D-Phe-Pro-Arg- Chloromethylketone, PDB code: 2thf was solved by S.Caccia, K.Futterer, E.Di Cera, G.Waksman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 53.100, 75.100, 81.400, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 26.5

Sodium Binding Sites:

The binding sites of Sodium atom in the Structure of Human Alpha-Thrombin Y225F Mutant Bound to D-Phe-Pro-Arg- Chloromethylketone (pdb code 2thf). 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 Human Alpha-Thrombin Y225F Mutant Bound to D-Phe-Pro-Arg- Chloromethylketone, PDB code: 2thf:

Sodium binding site 1 out of 1 in 2thf

Go back to Sodium Binding Sites List in 2thf
Sodium binding site 1 out of 1 in the Structure of Human Alpha-Thrombin Y225F Mutant Bound to D-Phe-Pro-Arg- Chloromethylketone


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of Human Alpha-Thrombin Y225F Mutant Bound to D-Phe-Pro-Arg- Chloromethylketone within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na2343

b:25.7
occ:1.00
 O B:ARG221A 2.4 24.1 1.0
O B:HOH1604 2.5 14.6 1.0
O B:LYS224 2.5 17.1 1.0
O B:HOH2191 2.6 14.2 1.0
O B:HOH5037 2.8 10.1 1.0
O B:HOH5269 2.8 20.9 1.0
C B:ARG221A 3.3 23.4 1.0
C B:LYS224 3.5 16.5 1.0
N B:LYS224 3.8 15.6 1.0
N B:ARG221A 3.8 20.6 1.0
C B:ASP221 3.9 21.7 1.0
O B:HOH5359 3.9 25.0 1.0
N B:ASP222 4.1 21.9 1.0
CA B:ASP222 4.1 20.1 1.0
O B:TYR184A 4.1 14.8 1.0
CA B:LYS224 4.1 16.5 1.0
CA B:ARG221A 4.2 20.4 1.0
O B:HOH5217 4.3 15.9 1.0
O B:ASP221 4.3 20.7 1.0
N B:GLY223 4.3 15.4 1.0
CA B:ASP221 4.3 21.0 1.0
C B:ASP222 4.4 18.8 1.0
CB B:LYS224 4.4 20.1 1.0
N B:PHE225 4.6 16.7 1.0
OD1 B:ASP221 4.6 16.9 1.0
O B:HOH6310 4.7 22.1 1.0
C B:GLY223 4.8 15.5 1.0
CA B:PHE225 4.9 13.4 1.0

Reference:

E.R.Guinto, S.Caccia, T.Rose, K.Futterer, G.Waksman, E.Di Cera. Unexpected Crucial Role of Residue 225 in Serine Proteases. Proc.Natl.Acad.Sci.Usa V. 96 1852 1999.
ISSN: ISSN 0027-8424
PubMed: 10051558
DOI: 10.1073/PNAS.96.5.1852
Page generated: Mon Oct 7 04:23:36 2024

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