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Chlorine in PDB 1b4t: H48C Yeast Cu(II)/Zn Superoxide Dismutase Room Temperature (298K) Structure

Enzymatic activity of H48C Yeast Cu(II)/Zn Superoxide Dismutase Room Temperature (298K) Structure

All present enzymatic activity of H48C Yeast Cu(II)/Zn Superoxide Dismutase Room Temperature (298K) Structure:
1.15.1.1;

Protein crystallography data

The structure of H48C Yeast Cu(II)/Zn Superoxide Dismutase Room Temperature (298K) Structure, PDB code: 1b4t was solved by P.J.Hart, M.M.Balbirnie, N.L.Ogihara, A.M.Nersissian, M.S.Weiss, J.S.Valentine, D.Eisenberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.80
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 118.647, 118.647, 75.376, 90.00, 90.00, 120.00
R / Rfree (%) 20.9 / 25.8

Other elements in 1b4t:

The structure of H48C Yeast Cu(II)/Zn Superoxide Dismutase Room Temperature (298K) Structure also contains other interesting chemical elements:

Copper (Cu) 1 atom
Zinc (Zn) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the H48C Yeast Cu(II)/Zn Superoxide Dismutase Room Temperature (298K) Structure (pdb code 1b4t). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the H48C Yeast Cu(II)/Zn Superoxide Dismutase Room Temperature (298K) Structure, PDB code: 1b4t:

Chlorine binding site 1 out of 1 in 1b4t

Go back to Chlorine Binding Sites List in 1b4t
Chlorine binding site 1 out of 1 in the H48C Yeast Cu(II)/Zn Superoxide Dismutase Room Temperature (298K) Structure


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of H48C Yeast Cu(II)/Zn Superoxide Dismutase Room Temperature (298K) Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl156

b:23.9
occ:1.00
CU A:CU154 2.1 20.2 1.0
NE2 A:HIS63 3.0 17.3 1.0
NE2 A:HIS120 3.1 19.3 1.0
CD2 A:HIS63 3.2 16.6 1.0
CE1 A:HIS120 3.3 17.6 1.0
NH2 A:ARG143 3.5 22.6 1.0
O A:HOH201 3.5 32.0 1.0
NE A:ARG143 3.6 20.6 1.0
CZ A:ARG143 3.7 20.2 1.0
SG A:CYS48 3.7 13.6 1.0
ND1 A:HIS46 4.1 16.5 1.0
CE1 A:HIS63 4.2 18.8 1.0
CD2 A:HIS120 4.4 18.1 1.0
O A:HOH223 4.5 38.0 1.0
NH1 A:ARG143 4.5 20.8 1.0
CG1 A:VAL118 4.5 18.4 1.0
O A:HOH203 4.5 40.9 1.0
CG A:HIS63 4.5 16.5 1.0
CD A:ARG143 4.5 19.7 1.0
ND1 A:HIS120 4.6 17.4 1.0
CG A:ARG143 4.7 19.9 1.0
CB A:HIS46 4.8 15.0 1.0
CG A:HIS46 4.9 15.7 1.0
O A:GLY61 4.9 16.6 1.0
CB A:VAL118 4.9 15.6 1.0
CE1 A:HIS46 5.0 16.2 1.0
ND1 A:HIS63 5.0 18.7 1.0

Reference:

P.J.Hart, M.M.Balbirnie, N.L.Ogihara, A.M.Nersissian, M.S.Weiss, J.S.Valentine, D.Eisenberg. A Structure-Based Mechanism For Copper-Zinc Superoxide Dismutase. Biochemistry V. 38 2167 1999.
ISSN: ISSN 0006-2960
PubMed: 10026301
DOI: 10.1021/BI982284U
Page generated: Sat Dec 12 08:31:45 2020

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