Zinc in PDB 4qtu: Crystal Structure of Rrna Modifying Enzyme

The structure of Crystal Structure of Rrna Modifying Enzyme, PDB code: 4qtu was solved by J.Letoquart, E.Huvelle, L.Wacheul, G.Bourgeois, C.Zorbas, M.Graille, V.Heurgue-Hamard, D.L.J.Lafontaine, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.31 / 2.12
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	75.472, 53.733, 85.205, 90.00, 94.55, 90.00
R / Rfree (%)	17.8 / 22.9

The binding sites of Zinc atom in the Crystal Structure of Rrna Modifying Enzyme (pdb code 4qtu). 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 Rrna Modifying Enzyme, PDB code: 4qtu:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Rrna Modifying Enzyme


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 Rrna Modifying Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn201 b:37.0 occ:1.00 SG A:CYS112 2.3 36.9 1.0 SG A:CYS16 2.3 33.9 1.0 SG A:CYS115 2.4 43.3 1.0 SG A:CYS11 2.4 33.1 1.0 CB A:CYS112 3.0 36.0 1.0 CB A:CYS115 3.2 39.5 1.0 CB A:CYS11 3.2 32.9 1.0 CB A:CYS16 3.4 38.7 1.0 N A:CYS115 3.7 44.1 1.0 CG1 A:VAL13 3.9 25.5 1.0 CA A:CYS115 4.0 41.5 1.0 CG2 A:VAL13 4.4 39.8 1.0 CA A:CYS112 4.5 39.7 1.0 CB A:ASN114 4.6 38.9 1.0 CB A:VAL13 4.7 41.0 1.0 CA A:CYS11 4.7 30.2 1.0 C A:ASN114 4.8 48.8 1.0 C A:CYS115 4.8 40.4 1.0 ND2 A:ASN114 4.8 41.5 1.0 CA A:CYS16 4.8 41.8 1.0 CB A:HIS117 5.0 39.3 1.0 N A:GLY116 5.0 41.0 1.0 N A:HIS117 5.0 43.8 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Rrna Modifying Enzyme


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 Rrna Modifying Enzyme within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn201 b:42.5 occ:1.00 SG C:CYS16 2.3 46.9 1.0 SG C:CYS11 2.4 43.8 1.0 SG C:CYS112 2.4 39.2 1.0 SG C:CYS115 2.4 51.2 1.0 CB C:CYS112 3.0 33.0 1.0 CB C:CYS11 3.2 41.2 1.0 CB C:CYS115 3.3 41.8 1.0 CB C:CYS16 3.4 44.8 1.0 N C:CYS115 3.7 45.6 1.0 CA C:CYS115 4.0 49.4 1.0 CB C:VAL13 4.1 40.3 1.0 CB C:ASN114 4.3 42.6 1.0 CG2 C:VAL13 4.4 39.3 1.0 CA C:CYS112 4.5 39.5 1.0 C C:ASN114 4.7 49.4 1.0 CA C:CYS11 4.7 37.7 1.0 CA C:CYS16 4.8 47.4 1.0 C C:CYS115 4.8 51.7 1.0 CG1 C:VAL13 4.8 43.7 1.0 ND2 C:ASN114 4.8 41.5 1.0 CA C:ASN114 4.9 49.5 1.0 N C:ASN114 4.9 49.2 1.0 N C:GLY116 4.9 42.7 1.0

J.Letoquart, E.Huvelle, L.Wacheul, G.Bourgeois, C.Zorbas, M.Graille, V.Heurgue-Hamard, D.L.J.Lafontaine. Structural and Functional Studies of BUD23-TRM112 Reveal 18S Rrna N7-G1575 Methylation Occurs on Late 40S Precursor Ribosomes Proc.Natl.Acad.Sci.Usa 2014.
ISSN: ESSN 1091-6490
PubMed: 25489090
DOI: 10.1073/PNAS.1413089111