Zinc in PDB 7fsf: Crystal Structure of T. Maritima Reverse Gyrase

All present enzymatic activity of Crystal Structure of T. Maritima Reverse Gyrase:
3.6.4.12; 5.6.2.2;

The structure of Crystal Structure of T. Maritima Reverse Gyrase, PDB code: 7fsf was solved by R.Rasche, D.Kummel, M.G.Rudolph, D.Klostermeier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	51.86 / 2.77
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	183.93, 103.26, 95.67, 90, 116.82, 90
R / Rfree (%)	21.9 / 27.3

The binding sites of Zinc atom in the Crystal Structure of T. Maritima Reverse Gyrase (pdb code 7fsf). 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 T. Maritima Reverse Gyrase, PDB code: 7fsf:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of T. Maritima Reverse Gyrase


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 T. Maritima Reverse Gyrase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1201 b:80.7 occ:1.00 SG A:CYS624 2.3 64.4 1.0 SG A:CYS638 2.3 80.4 1.0 SG A:CYS621 2.3 58.9 1.0 SG A:CYS635 2.4 91.7 1.0 CB A:CYS621 3.2 68.1 1.0 CB A:CYS635 3.3 84.5 1.0 CB A:CYS624 3.4 61.3 1.0 CB A:CYS638 3.7 87.2 1.0 N A:CYS638 3.9 80.9 1.0 N A:CYS624 4.0 64.9 1.0 CA A:CYS624 4.2 57.9 1.0 CA A:CYS638 4.3 77.8 1.0 CB A:VAL637 4.4 69.5 1.0 CB A:SER640 4.6 73.9 1.0 CA A:CYS621 4.7 62.0 1.0 CB A:TYR626 4.7 53.9 1.0 CA A:CYS635 4.8 90.8 1.0 C A:CYS624 4.8 56.2 1.0 N A:TYR626 4.9 64.0 1.0 N A:GLY625 4.9 63.3 1.0 C A:VAL637 4.9 91.0 1.0 C A:CYS638 4.9 85.5 1.0 N A:VAL637 4.9 82.2 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of T. Maritima Reverse Gyrase


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 T. Maritima Reverse Gyrase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1202 b:69.0 occ:1.00 SG A:CYS29 2.2 66.7 1.0 SG A:CYS14 2.2 62.5 1.0 SG A:CYS32 2.3 65.2 1.0 SG A:CYS11 2.3 52.4 1.0 CB A:CYS14 3.3 79.6 1.0 CB A:CYS29 3.3 64.0 1.0 CB A:CYS32 3.4 73.1 1.0 CB A:CYS11 3.4 65.6 1.0 N A:CYS14 3.7 71.3 1.0 N A:CYS29 3.8 67.8 1.0 CA A:CYS14 4.0 58.7 1.0 CA A:CYS29 4.1 64.5 1.0 N A:CYS32 4.1 66.4 1.0 CA A:CYS32 4.3 71.8 1.0 CB A:ASN13 4.5 52.5 1.0 C A:ASN13 4.7 61.9 1.0 CB A:PRO28 4.7 51.4 1.0 C A:CYS29 4.7 61.0 1.0 O A:CYS29 4.8 69.0 1.0 C A:CYS14 4.8 58.8 1.0 CA A:CYS11 4.8 48.2 1.0 C A:PRO28 4.9 61.6 1.0 N A:ASN13 4.9 72.1 1.0 CA A:ASN13 4.9 62.3 1.0

V.Mhaindarkar, R.Rasche, D.Kummel, M.G.Rudolph, D.Klostermeier. Structure of Reverse Gyrase with A Minimal Latch That Supports Atp-Dependent Positive Supercoiling Without Specific Interactions with the Topoisomerase Domain Acta Crystallogr.,Sect.D 2023.
ISSN: ESSN 1399-0047
DOI: 10.1107/S2059798323002565