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Sodium in PDB 2jh0: Human Thrombin Hirugen Inhibitor Complex

Enzymatic activity of Human Thrombin Hirugen Inhibitor Complex

All present enzymatic activity of Human Thrombin Hirugen Inhibitor Complex:
3.4.21.5;

Protein crystallography data

The structure of Human Thrombin Hirugen Inhibitor Complex, PDB code: 2jh0 was solved by S.Senger, C.Chan, M.A.Convery, J.A.Hubbard, R.J.Young, G.P.Shah, N.S.Watson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.70
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 70.070, 71.556, 71.931, 90.00, 100.12, 90.00
R / Rfree (%) 18.3 / 21

Other elements in 2jh0:

The structure of Human Thrombin Hirugen Inhibitor Complex also contains other interesting chemical elements:

Chlorine (Cl) 1 atom
Calcium (Ca) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Human Thrombin Hirugen Inhibitor Complex (pdb code 2jh0). 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 Human Thrombin Hirugen Inhibitor Complex, PDB code: 2jh0:

Sodium binding site 1 out of 1 in 2jh0

Go back to Sodium Binding Sites List in 2jh0
Sodium binding site 1 out of 1 in the Human Thrombin Hirugen Inhibitor Complex


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Human Thrombin Hirugen Inhibitor Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Na1249

b:27.6
occ:1.00
O D:ARG221 2.3 29.8 1.0
O D:HOH2164 2.3 28.6 1.0
O D:HOH2143 2.3 26.6 1.0
O D:LYS224 2.4 25.0 1.0
O D:HOH2133 2.6 25.7 1.0
O D:HOH2136 2.7 30.9 1.0
C D:ARG221 3.4 31.4 1.0
C D:LYS224 3.5 25.4 1.0
N D:ARG221 3.8 30.4 1.0
O D:HOH2141 3.9 26.0 1.0
N D:LYS224 3.9 26.0 1.0
O D:HOH2165 3.9 31.9 1.0
C D:ASP221A 4.0 30.4 1.0
O D:TYR184 4.1 29.0 1.0
CA D:LYS224 4.2 25.6 1.0
O D:HOH2142 4.2 26.6 1.0
CA D:ARG221 4.2 31.3 1.0
N D:ASP222 4.2 32.2 1.0
CA D:ASP221A 4.2 29.3 1.0
CA D:ASP222 4.3 33.5 1.0
N D:GLY223 4.4 32.8 1.0
N D:TYR225 4.5 23.3 1.0
O D:ASP221A 4.5 31.0 1.0
CB D:LYS224 4.5 27.3 1.0
C D:ASP222 4.5 33.3 1.0
OD1 D:ASP221A 4.6 28.5 1.0
CA D:TYR225 4.7 24.0 1.0
C D:GLY223 4.9 29.1 1.0
N D:ASP221A 5.0 27.4 1.0
O D:HOH2159 5.0 28.1 1.0

Reference:

S.Senger, C.Chan, M.A.Convery, J.A.Hubbard, G.P.Shah, N.S.Watson, R.J.Young. Sulfonamide-Related Conformational Effects and Their Importance in Structure-Based Design. Bioorg.Med.Chem.Lett. V. 17 2931 2007.
ISSN: ISSN 0960-894X
PubMed: 17336062
DOI: 10.1016/J.BMCL.2007.02.034
Page generated: Mon Oct 7 03:00:44 2024

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