Calcium in PDB 1hl5: The Structure of Holo Type Human Cu, Zn Superoxide Dismutase

All present enzymatic activity of The Structure of Holo Type Human Cu, Zn Superoxide Dismutase:
1.15.1.1;

The structure of The Structure of Holo Type Human Cu, Zn Superoxide Dismutase, PDB code: 1hl5 was solved by R.W.Strange, S.Antonyuk, M.A.Hough, P.Doucette, J.Rodriguez, P.J.Hart, L.J.Hayward, J.S.Valentine, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.8
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	76.871, 172.380, 112.450, 90.00, 93.45, 90.00
R / Rfree (%)	18.5 / 22.2

The structure of The Structure of Holo Type Human Cu, Zn Superoxide Dismutase also contains other interesting chemical elements:

Copper	(Cu)	18 atoms
Zinc	(Zn)	18 atoms

The binding sites of Calcium atom in the The Structure of Holo Type Human Cu, Zn Superoxide Dismutase (pdb code 1hl5). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the The Structure of Holo Type Human Cu, Zn Superoxide Dismutase, PDB code: 1hl5:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the The Structure of Holo Type Human Cu, Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of The Structure of Holo Type Human Cu, Zn Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca156 b:37.4 occ:0.50 O C:HOH2037 2.2 58.0 1.0 O C:HOH2035 2.3 70.3 1.0 O C:HOH2038 2.4 40.1 1.0 OD1 C:ASN26 2.4 26.9 1.0 O C:SER102 2.5 9.3 1.0 O C:ASN26 2.5 17.2 1.0 O C:HOH2106 2.7 47.1 1.0 O C:HOH2036 3.4 61.6 1.0 C C:ASN26 3.5 16.2 1.0 C C:SER102 3.6 8.4 1.0 CG C:ASN26 3.6 23.2 1.0 CA C:ASN26 4.0 17.6 1.0 O C:GLY27 4.2 11.2 1.0 CA C:SER102 4.2 9.3 1.0 CB C:SER102 4.3 11.4 1.0 CB C:ASN26 4.4 18.8 1.0 O C:ILE104 4.5 6.1 1.0 N C:GLY27 4.5 14.4 1.0 N C:VAL103 4.6 6.1 1.0 ND2 C:ASN26 4.7 26.3 1.0 C C:GLY27 4.7 10.9 1.0 O C:VAL103 4.7 5.0 1.0 O C:HOH2109 4.8 50.6 1.0 CA C:VAL103 4.8 5.2 1.0 CA C:GLY27 4.9 12.4 1.0 C C:VAL103 4.9 5.3 1.0

Calcium binding site 2 out of 3 in the The Structure of Holo Type Human Cu, Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of The Structure of Holo Type Human Cu, Zn Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca156 b:47.4 occ:1.00 O D:HOH2072 2.3 46.5 1.0 O D:HOH2024 2.4 40.8 1.0 OD1 D:ASN26 2.5 21.1 1.0 O D:SER102 2.6 14.7 1.0 O D:ASN26 2.7 16.9 1.0 CG D:ASN26 3.2 18.6 1.0 C D:ASN26 3.6 16.2 1.0 C D:SER102 3.7 12.8 1.0 ND2 D:ASN26 3.9 19.7 1.0 CA D:ASN26 4.0 16.9 1.0 CB D:ASN26 4.2 16.7 1.0 CA D:SER102 4.4 14.2 1.0 O D:GLY27 4.4 13.0 1.0 O D:ILE104 4.5 8.6 1.0 CB D:SER102 4.6 16.1 1.0 O D:VAL103 4.6 9.7 1.0 O D:HOH2073 4.6 47.9 1.0 N D:GLY27 4.7 15.8 1.0 N D:VAL103 4.7 11.3 1.0 CA D:VAL103 4.8 9.8 1.0 C D:VAL103 4.9 9.8 1.0 C D:GLY27 5.0 12.9 1.0 CB D:SER105 5.0 8.1 1.0

Calcium binding site 3 out of 3 in the The Structure of Holo Type Human Cu, Zn Superoxide Dismutase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of The Structure of Holo Type Human Cu, Zn Superoxide Dismutase within 5.0Å range: probe atom residue distance (Å) B Occ O:Ca156 b:45.0 occ:1.00 O H:HOH2084 2.4 41.1 1.0 O H:HOH2085 2.4 35.4 1.0 O H:HOH2081 2.4 52.2 1.0 O H:SER102 2.5 10.6 1.0 OD1 H:ASN26 2.6 21.2 1.0 O H:ASN26 2.7 10.7 1.0 CG H:ASN26 3.4 16.6 1.0 C H:SER102 3.6 10.1 1.0 C H:ASN26 3.6 11.5 1.0 ND2 H:ASN26 4.1 19.1 1.0 CA H:ASN26 4.1 11.9 1.0 CA H:SER102 4.3 10.8 1.0 O H:ILE104 4.3 7.6 1.0 O H:GLY27 4.3 8.6 1.0 CB H:ASN26 4.4 13.3 1.0 CB H:SER102 4.4 11.2 1.0 N H:VAL103 4.6 8.6 1.0 N H:GLY27 4.7 9.7 1.0 O H:HOH2080 4.7 54.2 1.0 O H:VAL103 4.7 8.3 1.0 CA H:VAL103 4.8 8.8 1.0 O H:HOH2086 4.8 50.0 1.0 C H:GLY27 4.8 9.0 1.0 C H:VAL103 4.9 8.2 1.0 CA H:GLY27 5.0 10.0 1.0

R.W.Strange, S.Antonyuk, M.A.Hough, P.Doucette, J.Rodriguez, P.J.Hart, L.J.Hayward, J.S.Valentine, S.S.Hasnain. The Structure of Holo and Metal-Deficient Wild-Type Human Cu, Zn Superoxide Dismutase and Its Relevance to Familial Amyotrophic Lateral Sclerosis J.Mol.Biol. V. 328 877 2003.
ISSN: ISSN 0022-2836
PubMed: 12729761
DOI: 10.1016/S0022-2836(03)00355-3