Zinc in PDB 7qy5: Crystal Structure of the S.Pombe ARS2-RED1 Complex.

The structure of Crystal Structure of the S.Pombe ARS2-RED1 Complex., PDB code: 7qy5 was solved by A.E.Foucher, J.Kadlec, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	84.85 / 2.77
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	64.67, 128.281, 89.261, 90, 108.08, 90
R / Rfree (%)	22.8 / 29.8

The binding sites of Zinc atom in the Crystal Structure of the S.Pombe ARS2-RED1 Complex. (pdb code 7qy5). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the S.Pombe ARS2-RED1 Complex., PDB code: 7qy5:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of the S.Pombe ARS2-RED1 Complex.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the S.Pombe ARS2-RED1 Complex. within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn601 b:70.2 occ:1.00 SG B:CYS476 2.0 80.7 1.0 NE2 B:HIS494 2.1 75.5 1.0 NE2 B:HIS499 2.3 61.6 1.0 SG B:CYS481 2.3 73.8 1.0 CD2 B:HIS494 3.0 74.6 1.0 CB B:CYS476 3.0 81.5 1.0 CB B:CYS481 3.0 73.9 1.0 CD2 B:HIS499 3.1 62.1 1.0 CE1 B:HIS494 3.2 74.8 1.0 CE1 B:HIS499 3.5 63.2 1.0 CG B:HIS494 4.1 71.4 1.0 ND1 B:HIS494 4.2 71.3 1.0 O B:CYS476 4.2 93.7 1.0 CG B:HIS499 4.3 60.4 1.0 CA B:CYS476 4.3 84.4 1.0 C B:CYS476 4.4 88.7 1.0 ND1 B:HIS499 4.4 60.6 1.0 CA B:CYS481 4.5 74.0 1.0 O B:VAL478 4.5 71.3 1.0 CD B:LYS498 4.5 88.5 1.0 NZ B:LYS498 4.7 83.9 1.0 CB B:VAL478 4.8 59.6 1.0 CD1 B:ILE495 4.8 61.3 1.0 CB B:LYS483 4.9 77.9 1.0 C B:CYS481 5.0 76.9 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of the S.Pombe ARS2-RED1 Complex.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the S.Pombe ARS2-RED1 Complex. within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn601 b:64.7 occ:1.00 CE1 D:HIS499 2.3 67.7 1.0 CE1 D:HIS494 2.4 81.7 1.0 SG D:CYS476 2.4 84.6 1.0 SG D:CYS481 2.5 73.2 1.0 NE2 D:HIS499 2.6 68.4 1.0 ND1 D:HIS494 2.7 77.9 1.0 CB D:CYS476 3.2 88.3 1.0 CB D:CYS481 3.3 76.2 1.0 NE2 D:HIS494 3.4 86.6 1.0 ND1 D:HIS499 3.4 69.7 1.0 CD2 D:HIS499 3.8 64.7 1.0 CG D:HIS494 3.9 79.7 1.0 CD2 D:HIS494 4.2 83.0 1.0 CG D:HIS499 4.2 65.5 1.0 O D:VAL478 4.4 75.2 1.0 CA D:CYS476 4.6 95.2 1.0 CB D:VAL478 4.6 68.2 1.0 CA D:CYS481 4.7 78.5 1.0 CE D:LYS498 4.8 90.0 1.0 NZ D:LYS498 4.9 88.9 1.0 N D:VAL478 5.0 68.2 1.0 C D:CYS476 5.0 91.0 1.0 CG1 D:ILE495 5.0 69.7 1.0

A.E.Foucher, L.Touat-Todeschini, A.B.Juarez-Martinez, A.Rakitch, H.Laroussi, C.Karczewski, S.Acajjaoui, M.Soler-Lopez, S.Cusack, C.D.Mackereth, A.Verdel, J.Kadlec. Structural Analysis of RED1 As A Conserved Scaffold of the Rna-Targeting Mtrec/Paxt Complex. Nat Commun V. 13 4969 2022.
ISSN: ESSN 2041-1723
PubMed: 36002457
DOI: 10.1038/S41467-022-32542-3