Zinc in PDB 6fon: Elongated Conformer of the Human Copper Chaperone For SOD1 Complexed with Human SOD1

All present enzymatic activity of Elongated Conformer of the Human Copper Chaperone For SOD1 Complexed with Human SOD1:
1.15.1.1;

The structure of Elongated Conformer of the Human Copper Chaperone For SOD1 Complexed with Human SOD1, PDB code: 6fon was solved by G.S.A.Wright, F.A.Sala, S.V.Antonyuk, R.C.Garratt, S.S.Hasnain, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.19 / 3.05
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	172.481, 172.481, 219.244, 90.00, 90.00, 120.00
R / Rfree (%)	19.9 / 24.6

The binding sites of Zinc atom in the Elongated Conformer of the Human Copper Chaperone For SOD1 Complexed with Human SOD1 (pdb code 6fon). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Elongated Conformer of the Human Copper Chaperone For SOD1 Complexed with Human SOD1, PDB code: 6fon:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Elongated Conformer of the Human Copper Chaperone For SOD1 Complexed with Human SOD1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Elongated Conformer of the Human Copper Chaperone For SOD1 Complexed with Human SOD1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn501 b:70.5 occ:1.00 ND1 A:HIS164 2.0 65.6 1.0 OD1 A:ASP167 2.1 59.7 1.0 ND1 A:HIS147 2.1 66.0 1.0 ND1 A:HIS155 2.1 88.9 1.0 CG A:ASP167 2.8 65.8 1.0 CE1 A:HIS164 2.8 70.5 1.0 OD2 A:ASP167 2.8 62.3 1.0 CG A:HIS164 2.9 69.6 1.0 CG A:HIS147 3.1 72.9 1.0 CE1 A:HIS155 3.1 86.1 1.0 CE1 A:HIS147 3.1 74.6 1.0 CG A:HIS155 3.2 73.2 1.0 CB A:HIS147 3.3 75.6 1.0 CB A:HIS164 3.4 70.8 1.0 CB A:HIS155 3.5 70.0 1.0 NE2 A:HIS164 3.8 71.2 1.0 CA A:HIS155 3.9 70.9 1.0 CD2 A:HIS164 3.9 71.2 1.0 O A:ILE217 4.0 0.4 1.0 CD2 A:HIS147 4.2 71.6 1.0 NE2 A:HIS155 4.2 80.2 1.0 NE2 A:HIS147 4.2 74.9 1.0 CD2 A:HIS155 4.3 77.0 1.0 CB A:ASP167 4.3 63.8 1.0 CA A:HIS164 4.7 71.5 1.0 N A:GLY156 4.7 70.0 1.0 N A:HIS164 4.8 73.6 1.0 C A:ILE217 4.8 92.3 1.0 CA A:HIS147 4.8 76.4 1.0 N A:HIS155 4.9 73.3 1.0 C A:HIS155 4.9 70.2 1.0 CA A:ASP167 4.9 65.6 1.0 CA A:THR218 5.0 81.0 1.0 CD2 A:HIS130 5.0 88.0 1.0

Zinc binding site 2 out of 4 in the Elongated Conformer of the Human Copper Chaperone For SOD1 Complexed with Human SOD1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Elongated Conformer of the Human Copper Chaperone For SOD1 Complexed with Human SOD1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn201 b:70.9 occ:1.00 OD1 B:ASP83 1.9 74.4 1.0 ND1 B:HIS80 2.1 76.1 1.0 ND1 B:HIS71 2.1 91.0 1.0 ND1 B:HIS63 2.2 80.0 1.0 OD2 B:ASP83 2.6 69.5 1.0 CG B:ASP83 2.6 74.3 1.0 CE1 B:HIS80 3.0 76.5 1.0 CE1 B:HIS71 3.0 92.0 1.0 CG B:HIS80 3.1 75.9 1.0 CG B:HIS71 3.2 90.0 1.0 CG B:HIS63 3.2 79.2 1.0 CE1 B:HIS63 3.2 85.9 1.0 CB B:HIS63 3.5 76.7 1.0 CB B:HIS80 3.5 72.3 1.0 CB B:HIS71 3.6 87.4 1.0 O B:LYS136 3.8 88.8 1.0 CA B:HIS71 3.9 83.3 1.0 NE2 B:HIS80 4.0 76.8 1.0 CB B:ASP83 4.1 76.9 1.0 CD2 B:HIS80 4.1 76.3 1.0 NE2 B:HIS71 4.1 90.6 1.0 CD2 B:HIS71 4.2 90.5 1.0 NE2 B:HIS63 4.3 86.3 1.0 CD2 B:HIS63 4.3 85.0 1.0 N B:GLY72 4.6 86.4 1.0 N B:HIS80 4.6 67.7 1.0 CA B:HIS80 4.7 67.8 1.0 CA B:ASP83 4.7 78.8 1.0 C B:HIS71 4.8 79.5 1.0 C B:LYS136 4.8 86.8 1.0 N B:ASP83 4.9 76.5 1.0 N B:HIS71 4.9 84.5 1.0 CA B:HIS63 5.0 71.8 1.0

Zinc binding site 3 out of 4 in the Elongated Conformer of the Human Copper Chaperone For SOD1 Complexed with Human SOD1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Elongated Conformer of the Human Copper Chaperone For SOD1 Complexed with Human SOD1 within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn301 b:67.0 occ:1.00 OD1 C:ASP167 1.9 73.7 1.0 ND1 C:HIS164 2.1 77.2 1.0 ND1 C:HIS147 2.1 65.8 1.0 ND1 C:HIS155 2.1 57.7 1.0 CG C:ASP167 2.7 68.5 1.0 OD2 C:ASP167 2.8 64.6 1.0 CE1 C:HIS164 2.9 74.7 1.0 CG C:HIS164 3.0 86.5 1.0 CE1 C:HIS155 3.0 59.9 1.0 CE1 C:HIS147 3.1 69.8 1.0 CG C:HIS147 3.1 60.6 1.0 CG C:HIS155 3.2 68.7 1.0 CB C:HIS147 3.4 64.2 1.0 CB C:HIS164 3.4 89.8 1.0 CB C:HIS155 3.5 71.9 1.0 CA C:HIS155 3.9 75.0 1.0 NE2 C:HIS164 3.9 80.6 1.0 CD2 C:HIS164 4.0 83.7 1.0 O C:ILE217 4.0 81.8 1.0 NE2 C:HIS155 4.1 65.2 1.0 NE2 C:HIS147 4.2 74.8 1.0 CB C:ASP167 4.2 68.0 1.0 CD2 C:HIS147 4.2 62.0 1.0 CD2 C:HIS155 4.2 68.7 1.0 CA C:HIS164 4.7 85.0 1.0 N C:GLY156 4.7 79.5 1.0 N C:HIS164 4.8 76.5 1.0 CA C:ASP167 4.8 65.2 1.0 C C:ILE217 4.8 74.1 1.0 C C:HIS155 4.9 77.0 1.0 CD2 C:HIS130 4.9 66.1 1.0 CA C:HIS147 4.9 67.9 1.0 N C:ASP167 4.9 60.8 1.0 N C:HIS155 4.9 81.3 1.0 CA C:THR218 5.0 60.9 1.0

Zinc binding site 4 out of 4 in the Elongated Conformer of the Human Copper Chaperone For SOD1 Complexed with Human SOD1


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Elongated Conformer of the Human Copper Chaperone For SOD1 Complexed with Human SOD1 within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn201 b:97.9 occ:1.00 OD1 D:ASP83 2.0 95.3 1.0 ND1 D:HIS80 2.0 98.6 1.0 ND1 D:HIS63 2.0 94.8 1.0 ND1 D:HIS71 2.3 0.1 1.0 CG D:ASP83 2.8 87.8 1.0 OD2 D:ASP83 2.8 75.3 1.0 CE1 D:HIS80 2.9 0.3 1.0 CG D:HIS63 2.9 91.5 1.0 CG D:HIS80 3.1 99.3 1.0 CE1 D:HIS63 3.1 0.6 1.0 CE1 D:HIS71 3.2 0.2 1.0 CB D:HIS63 3.2 88.3 1.0 CG D:HIS71 3.3 1.0 1.0 CB D:HIS80 3.5 100.0 1.0 O D:LYS136 3.7 0.3 1.0 CB D:HIS71 3.7 0.7 1.0 NE2 D:HIS80 4.0 0.6 1.0 CA D:HIS71 4.1 0.3 1.0 CD2 D:HIS80 4.1 0.7 1.0 CD2 D:HIS63 4.1 99.5 1.0 NE2 D:HIS63 4.2 0.1 1.0 CB D:ASP83 4.2 93.0 1.0 NE2 D:HIS71 4.3 0.1 1.0 CD2 D:HIS71 4.4 1.0 1.0 CA D:HIS63 4.7 85.0 1.0 CA D:HIS80 4.7 95.6 1.0 N D:HIS80 4.8 0.1 1.0 C D:LYS136 4.8 0.3 1.0 CA D:ASP83 4.8 93.7 1.0 N D:GLY72 4.9 0.3 1.0 N D:ASP83 4.9 93.9 1.0

F.A.Sala, G.S.A.Wright, S.V.Antonyuk, R.C.Garratt, S.S.Hasnain. Molecular Recognition and Maturation of SOD1 By Its Evolutionarily Destabilised Cognate Chaperone Hccs. Plos Biol. V. 17 00141 2019.
ISSN: ESSN 1545-7885
PubMed: 30735496
DOI: 10.1371/JOURNAL.PBIO.3000141