Atomistry » Sodium » PDB 1b7s-1c82 » 1c1v
Atomistry »
  Sodium »
    PDB 1b7s-1c82 »
      1c1v »

Sodium in PDB 1c1v: Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases

Enzymatic activity of Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases

All present enzymatic activity of Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases:
3.4.21.5;

Protein crystallography data

The structure of Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases, PDB code: 1c1v was solved by B.A.Katz, C.Luong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.50 / 1.98
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 72.470, 72.090, 73.110, 90.00, 101.51, 90.00
R / Rfree (%) 20.4 / 24.8

Other elements in 1c1v:

The structure of Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases (pdb code 1c1v). 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 Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases, PDB code: 1c1v:

Sodium binding site 1 out of 1 in 1c1v

Go back to Sodium Binding Sites List in 1c1v
Sodium binding site 1 out of 1 in the Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Na409

b:39.9
occ:1.00
 O H:ARG227A 2.4 19.6 1.0
O H:LYS230 2.4 19.5 1.0
O H:HOH452 2.6 35.2 1.0
O H:HOH454 2.6 15.5 1.0
O H:HOH428 2.7 14.1 1.0
H1 H:HOH428 2.9 13.5 1.0
O H:HOH431 2.9 13.3 1.0
H1 H:HOH452 3.0 35.6 1.0
H1 H:HOH454 3.0 17.1 1.0
H2 H:HOH431 3.1 11.8 1.0
H H:LYS230 3.3 29.2 1.0
H2 H:HOH452 3.3 38.5 1.0
H2 H:HOH428 3.3 11.1 1.0
H2 H:HOH439 3.3 26.2 1.0
H2 H:HOH454 3.4 19.1 1.0
H1 H:HOH431 3.4 7.8 1.0
HA H:ASP228 3.4 27.9 1.0
C H:LYS230 3.4 21.9 1.0
HA H:ASP227 3.5 19.4 1.0
H1 H:HOH422 3.5 32.8 1.0
C H:ARG227A 3.5 20.0 1.0
H H:GLY229 3.6 31.3 1.0
HB2 H:LYS230 3.7 25.5 1.0
O H:HOH439 3.7 25.7 1.0
N H:LYS230 3.8 27.8 1.0
O H:HOH441 3.9 2.6 1.0
N H:ARG227A 3.9 19.1 1.0
C H:ASP227 4.0 18.8 1.0
HA H:TYR231 4.0 14.4 1.0
H H:ARG227A 4.0 16.5 1.0
CA H:LYS230 4.1 23.2 1.0
N H:GLY229 4.2 31.3 1.0
CA H:ASP228 4.2 28.6 1.0
CA H:ASP227 4.2 18.9 1.0
O H:HOH422 4.3 31.6 1.0
O H:ASP227 4.3 21.8 1.0
N H:ASP228 4.3 24.8 1.0
H1 H:HOH439 4.4 26.6 1.0
N H:TYR231 4.4 14.9 1.0
CA H:ARG227A 4.4 19.9 1.0
CB H:LYS230 4.4 26.5 1.0
O H:TYR190A 4.4 23.1 1.0
H1 H:HOH435 4.5 33.7 1.0
C H:ASP228 4.5 30.2 1.0
H1 H:HOH441 4.5 7.0 1.0
OD1 H:ASP227 4.6 18.9 1.0
H2 H:HOH422 4.6 34.7 1.0
H2 H:HOH441 4.6 8.9 1.0
CA H:TYR231 4.7 16.0 1.0
HB2 H:ARG227A 4.7 20.5 1.0
O H:HOH435 4.7 34.1 1.0
H H:TYR190A 4.8 6.2 1.0
C H:GLY229 4.8 30.7 1.0
HB2 H:ASP195 4.8 13.7 1.0
H H:ASP227 4.9 19.9 1.0
HA3 H:GLY189 4.9 4.5 1.0
HB3 H:LYS230 4.9 24.8 1.0

Reference:

B.A.Katz, J.M.Clark, J.S.Finer-Moore, T.E.Jenkins, C.R.Johnson, M.J.Ross, C.Luong, W.R.Moore, R.M.Stroud. Design of Potent Selective Zinc-Mediated Serine Protease Inhibitors. Nature V. 391 608 1998.
ISSN: ISSN 0028-0836
PubMed: 9468142
DOI: 10.1038/35422
Page generated: Sun Oct 6 17:56:47 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy