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Copper in PDB 1b4l: 15 Atmosphere Oxygen Yeast Cu/Zn Superoxide Dismutase Room Temperature (298K) Structure

Enzymatic activity of 15 Atmosphere Oxygen Yeast Cu/Zn Superoxide Dismutase Room Temperature (298K) Structure

All present enzymatic activity of 15 Atmosphere Oxygen Yeast Cu/Zn Superoxide Dismutase Room Temperature (298K) Structure:
1.15.1.1;

Protein crystallography data

The structure of 15 Atmosphere Oxygen Yeast Cu/Zn Superoxide Dismutase Room Temperature (298K) Structure, PDB code: 1b4l 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 (°) 118.900, 118.900, 75.200, 90.00, 90.00, 120.00
R / Rfree (%) 20 / 25.4

Other elements in 1b4l:

The structure of 15 Atmosphere Oxygen Yeast Cu/Zn Superoxide Dismutase Room Temperature (298K) Structure also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Copper Binding Sites:

The binding sites of Copper atom in the 15 Atmosphere Oxygen Yeast Cu/Zn Superoxide Dismutase Room Temperature (298K) Structure (pdb code 1b4l). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the 15 Atmosphere Oxygen Yeast Cu/Zn Superoxide Dismutase Room Temperature (298K) Structure, PDB code: 1b4l:

Copper binding site 1 out of 1 in 1b4l

Go back to Copper Binding Sites List in 1b4l
Copper binding site 1 out of 1 in the 15 Atmosphere Oxygen Yeast Cu/Zn Superoxide Dismutase Room Temperature (298K) Structure


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of 15 Atmosphere Oxygen Yeast Cu/Zn Superoxide Dismutase Room Temperature (298K) Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu154

b:22.0
occ:1.00
 NE2 A:HIS120 2.0 11.9 1.0
ND1 A:HIS46 2.1 13.3 1.0
NE2 A:HIS48 2.2 13.7 1.0
NE2 A:HIS63 2.7 16.2 1.0
CG A:HIS46 3.0 12.3 1.0
CD2 A:HIS120 3.0 10.0 1.0
CE1 A:HIS120 3.0 10.8 1.0
CE1 A:HIS48 3.1 13.8 1.0
CE1 A:HIS46 3.1 14.6 1.0
O A:HOH201 3.2 41.1 1.0
CB A:HIS46 3.2 11.7 1.0
O A:HOH200 3.2 27.1 1.0
CD2 A:HIS63 3.2 15.0 1.0
CD2 A:HIS48 3.3 13.6 1.0
CE1 A:HIS63 3.8 14.2 1.0
ND1 A:HIS120 4.1 11.4 1.0
CG A:HIS120 4.1 10.4 1.0
CD2 A:HIS46 4.1 12.7 1.0
NE2 A:HIS46 4.2 13.1 1.0
ND1 A:HIS48 4.3 13.6 1.0
CG A:HIS48 4.4 13.2 1.0
CA A:HIS46 4.4 10.5 1.0
CG A:HIS63 4.5 12.6 1.0
N A:HIS46 4.5 10.0 1.0
CB A:VAL118 4.5 12.5 1.0
CG1 A:VAL118 4.5 12.1 1.0
ND1 A:HIS63 4.7 13.9 1.0
O A:VAL118 4.8 12.7 1.0
C A:HIS46 4.9 9.7 1.0
O A:HIS46 5.0 10.2 1.0
O A:HOH223 5.0 32.1 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: Tue Jul 30 21:37:14 2024

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