Zinc in PDB 1do5: Human Copper Chaperone For Superoxide Dismutase Domain II

The structure of Human Copper Chaperone For Superoxide Dismutase Domain II, PDB code: 1do5 was solved by A.L.Lamb, A.K.Wernimont, R.A.Pufahl, T.V.O'halloran, A.C.Rosenzweig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.21 / 2.75
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	117.186, 66.716, 88.033, 90.00, 96.63, 90.00
R / Rfree (%)	22.8 / 28.3

The binding sites of Zinc atom in the Human Copper Chaperone For Superoxide Dismutase Domain II (pdb code 1do5). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Human Copper Chaperone For Superoxide Dismutase Domain II, PDB code: 1do5:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Human Copper Chaperone For Superoxide Dismutase Domain II


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Copper Chaperone For Superoxide Dismutase Domain II within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn28 b:28.4 occ:1.00 ND1 A:HIS147 2.1 19.1 1.0 OD1 A:ASP167 2.1 21.0 1.0 ND1 A:HIS155 2.1 29.9 1.0 ND1 A:HIS164 2.3 25.9 1.0 CG A:ASP167 2.8 20.2 1.0 OD2 A:ASP167 2.9 18.5 1.0 CE1 A:HIS155 3.0 29.1 1.0 CE1 A:HIS147 3.1 18.9 1.0 CG A:HIS147 3.1 20.0 1.0 CE1 A:HIS164 3.2 26.1 1.0 CG A:HIS155 3.2 30.0 1.0 CG A:HIS164 3.2 26.0 1.0 CB A:HIS147 3.4 21.0 1.0 CB A:HIS164 3.6 24.8 1.0 CB A:HIS155 3.6 28.2 1.0 O A:ILE217 3.9 27.2 1.0 CA A:HIS155 3.9 28.3 1.0 NE2 A:HIS155 4.2 30.1 1.0 NE2 A:HIS147 4.2 20.2 1.0 NE2 A:HIS164 4.2 26.8 1.0 CD2 A:HIS147 4.2 19.1 1.0 CD2 A:HIS164 4.3 25.9 1.0 CB A:ASP167 4.3 21.2 1.0 CD2 A:HIS155 4.3 30.7 1.0 CD2 A:HIS130 4.5 14.1 1.0 N A:GLY156 4.7 27.0 1.0 CA A:ASP167 4.8 20.6 1.0 N A:HIS155 4.9 29.8 1.0 N A:HIS164 4.9 26.7 1.0 CA A:HIS164 4.9 26.6 1.0 C A:ILE217 4.9 25.6 1.0 C A:HIS155 4.9 27.9 1.0 CA A:HIS147 4.9 23.4 1.0

Zinc binding site 2 out of 4 in the Human Copper Chaperone For Superoxide Dismutase Domain II


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human Copper Chaperone For Superoxide Dismutase Domain II within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn29 b:25.9 occ:1.00 OD1 B:ASP167 2.0 32.0 1.0 ND1 B:HIS155 2.1 36.1 1.0 ND1 B:HIS147 2.1 22.8 1.0 ND1 B:HIS164 2.3 24.6 1.0 CG B:ASP167 2.6 30.6 1.0 OD2 B:ASP167 2.7 32.2 1.0 CE1 B:HIS155 2.9 37.8 1.0 CE1 B:HIS147 3.0 24.2 1.0 CE1 B:HIS164 3.1 23.6 1.0 CG B:HIS147 3.2 22.4 1.0 CG B:HIS155 3.2 37.6 1.0 CG B:HIS164 3.3 26.0 1.0 CB B:HIS147 3.5 21.5 1.0 CB B:HIS155 3.7 36.7 1.0 CB B:HIS164 3.7 26.3 1.0 CA B:HIS155 3.9 34.9 1.0 CB B:ASP167 3.9 30.3 1.0 O B:ILE217 4.0 19.9 1.0 NE2 B:HIS155 4.1 38.4 1.0 NE2 B:HIS147 4.1 25.9 1.0 NE2 B:HIS164 4.2 25.1 1.0 CD2 B:HIS147 4.2 24.7 1.0 CD2 B:HIS155 4.2 38.5 1.0 CD2 B:HIS164 4.3 25.0 1.0 O B:THR218 4.6 26.2 1.0 CA B:ASP167 4.7 29.5 1.0 ND1 B:HIS130 4.7 16.9 1.0 N B:GLY156 4.8 33.5 1.0 CA B:THR218 4.8 23.6 1.0 N B:HIS155 4.8 33.4 1.0 C B:HIS155 4.9 34.4 1.0 C B:THR218 4.9 25.9 1.0 C B:ILE217 4.9 20.7 1.0 N B:HIS164 4.9 28.5 1.0 CA B:HIS164 5.0 27.6 1.0

Zinc binding site 3 out of 4 in the Human Copper Chaperone For Superoxide Dismutase Domain II


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Human Copper Chaperone For Superoxide Dismutase Domain II within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn30 b:28.6 occ:1.00 ND1 C:HIS164 2.1 22.6 1.0 ND1 C:HIS155 2.2 23.1 1.0 OD1 C:ASP167 2.2 21.8 1.0 ND1 C:HIS147 2.3 22.0 1.0 CE1 C:HIS164 2.8 21.1 1.0 CG C:ASP167 2.9 22.4 1.0 OD2 C:ASP167 2.9 21.7 1.0 CE1 C:HIS155 2.9 22.9 1.0 CG C:HIS147 3.1 21.0 1.0 CG C:HIS164 3.2 24.8 1.0 CE1 C:HIS147 3.3 23.1 1.0 CB C:HIS147 3.3 20.2 1.0 CG C:HIS155 3.3 24.3 1.0 CB C:HIS164 3.7 26.2 1.0 CB C:HIS155 3.8 24.5 1.0 NE2 C:HIS164 3.9 23.7 1.0 CA C:HIS155 4.1 25.2 1.0 CD2 C:HIS164 4.1 23.9 1.0 NE2 C:HIS155 4.1 23.5 1.0 O C:ILE217 4.1 26.6 1.0 CD2 C:HIS147 4.3 21.7 1.0 CB C:ASP167 4.3 22.7 1.0 NE2 C:HIS147 4.3 24.2 1.0 CD2 C:HIS155 4.4 23.8 1.0 ND1 C:HIS130 4.4 20.7 1.0 CA C:THR218 4.7 24.3 1.0 CA C:HIS147 4.8 21.6 1.0 CE1 C:HIS130 4.8 19.1 1.0 N C:GLY156 4.9 27.3 1.0 O C:THR218 4.9 24.6 1.0 C C:ILE217 4.9 25.3 1.0 CA C:ASP167 4.9 23.3 1.0 N C:HIS164 5.0 31.3 1.0 CA C:HIS164 5.0 28.2 1.0

Zinc binding site 4 out of 4 in the Human Copper Chaperone For Superoxide Dismutase Domain II


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Human Copper Chaperone For Superoxide Dismutase Domain II within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn27 b:28.5 occ:1.00 OD1 D:ASP167 2.1 21.3 1.0 ND1 D:HIS155 2.2 27.4 1.0 ND1 D:HIS147 2.2 21.9 1.0 ND1 D:HIS164 2.6 33.9 1.0 CG D:ASP167 2.8 20.5 1.0 OD2 D:ASP167 2.8 17.9 1.0 CG D:HIS147 2.9 22.1 1.0 CE1 D:HIS155 3.0 25.2 1.0 CB D:HIS147 3.0 25.1 1.0 CG D:HIS155 3.3 28.3 1.0 CE1 D:HIS147 3.3 22.0 1.0 CE1 D:HIS164 3.3 33.1 1.0 CG D:HIS164 3.4 32.1 1.0 CB D:HIS155 3.7 25.3 1.0 CB D:HIS164 3.7 29.9 1.0 CA D:HIS155 4.0 26.5 1.0 O D:ILE217 4.0 29.7 1.0 NE2 D:HIS155 4.1 25.8 1.0 CD2 D:HIS147 4.2 21.8 1.0 NE2 D:HIS164 4.2 32.6 1.0 CB D:ASP167 4.2 21.1 1.0 CD2 D:HIS164 4.3 32.7 1.0 NE2 D:HIS147 4.3 22.5 1.0 CD2 D:HIS155 4.3 28.1 1.0 CA D:HIS147 4.6 28.0 1.0 O D:THR218 4.7 30.0 1.0 CA D:ASP167 4.8 22.2 1.0 N D:GLY156 4.8 24.9 1.0 N D:HIS164 4.9 28.8 1.0 ND1 D:HIS130 4.9 16.6 1.0 N D:HIS155 4.9 29.6 1.0 CA D:HIS164 5.0 30.0 1.0 C D:HIS155 5.0 26.2 1.0

A.L.Lamb, A.K.Wernimont, R.A.Pufahl, T.V.O'halloran, A.C.Rosenzweig. Crystal Structure of the Second Domain of the Human Copper Chaperone For Superoxide Dismutase. Biochemistry V. 39 1589 2000.
ISSN: ISSN 0006-2960
PubMed: 10677207
DOI: 10.1021/BI992822I