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Sodium in PDB 1c1w: 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: 1c1w 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 / 1.90
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 71.220, 71.880, 72.650, 90.00, 100.69, 90.00
R / Rfree (%) 20.3 / 24.2

Other elements in 1c1w:

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

Zinc (Zn) 3 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Recruiting Zinc to Mediate Potent, Specific Inhibition of Serine Proteases (pdb code 1c1w). 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: 1c1w:

Sodium binding site 1 out of 1 in 1c1w

Go back to Sodium Binding Sites List in 1c1w
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:34.8
occ:1.00
 O H:LYS230 2.3 25.2 1.0
O H:ARG227A 2.4 26.9 1.0
O H:HOH452 2.5 44.6 1.0
O H:HOH454 2.5 49.0 1.0
O H:HOH428 2.6 25.1 1.0
O H:HOH431 2.6 21.3 1.0
H1 H:HOH428 2.8 26.4 1.0
H1 H:HOH452 2.9 43.3 1.0
H1 H:HOH454 2.9 48.5 1.0
H H:LYS230 2.9 27.4 1.0
H2 H:HOH431 3.0 17.0 1.0
H1 H:HOH431 3.1 20.5 1.0
H2 H:HOH428 3.1 18.7 1.0
HA H:ASP228 3.2 32.9 1.0
H2 H:HOH452 3.2 40.7 1.0
C H:LYS230 3.3 27.8 1.0
H2 H:HOH454 3.4 47.8 1.0
H2 H:HOH438 3.5 22.1 1.0
C H:ARG227A 3.5 27.8 1.0
N H:LYS230 3.6 26.7 1.0
H1 H:HOH422 3.6 24.9 1.0
H H:GLY229 3.6 36.6 1.0
HB2 H:LYS230 3.6 30.0 1.0
HA H:TYR231 3.8 20.6 1.0
HA H:ASP227 3.9 24.1 1.0
O H:HOH440 3.9 35.0 1.0
CA H:LYS230 3.9 28.8 1.0
O H:HOH438 4.0 21.6 1.0
CA H:ASP228 4.0 33.0 1.0
N H:GLY229 4.0 39.1 1.0
H H:ARG227A 4.1 25.5 1.0
O H:TYR190A 4.1 19.9 1.0
N H:ARG227A 4.1 26.1 1.0
C H:ASP228 4.2 38.7 1.0
H1 H:HOH435 4.3 19.9 1.0
N H:ASP228 4.3 30.9 1.0
N H:TYR231 4.3 19.5 1.0
CB H:LYS230 4.3 30.9 1.0
C H:ASP227 4.4 25.4 1.0
O H:HOH422 4.5 22.1 1.0
H1 H:HOH438 4.5 20.5 1.0
CA H:ARG227A 4.6 24.2 1.0
H1 H:HOH440 4.6 32.2 1.0
CA H:TYR231 4.6 20.6 1.0
C H:GLY229 4.6 32.5 1.0
CA H:ASP227 4.7 21.9 1.0
H2 H:HOH440 4.7 34.5 1.0
HB2 H:ARG227A 4.8 29.4 1.0
CD1 H:TYR231 4.8 13.5 1.0
O H:HOH435 4.8 20.8 1.0
H2 H:HOH422 4.8 21.5 1.0
HB3 H:LYS230 4.8 32.5 1.0
HD1 H:TYR231 4.8 14.6 1.0
HA3 H:GLY189 4.9 13.7 1.0
O H:ASP227 4.9 25.4 1.0
OD1 H:ASP227 4.9 32.8 1.0
CA H:GLY229 4.9 34.1 1.0
CE1 H:TYR231 4.9 17.3 1.0
H H:TYR190A 4.9 15.6 1.0
HA H:LYS230 4.9 30.1 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 17:57:04 2024

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