Zinc in PDB 6zuo: Human RIO1(Kd)-Stha Late Pre-40S Particle, Structural State A (Pre 18S Rrna Cleavage)

All present enzymatic activity of Human RIO1(Kd)-Stha Late Pre-40S Particle, Structural State A (Pre 18S Rrna Cleavage):
4.2.99.18;

The binding sites of Zinc atom in the Human RIO1(Kd)-Stha Late Pre-40S Particle, Structural State A (Pre 18S Rrna Cleavage) (pdb code 6zuo). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Human RIO1(Kd)-Stha Late Pre-40S Particle, Structural State A (Pre 18S Rrna Cleavage), PDB code: 6zuo:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Human RIO1(Kd)-Stha Late Pre-40S Particle, Structural State A (Pre 18S Rrna Cleavage)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human RIO1(Kd)-Stha Late Pre-40S Particle, Structural State A (Pre 18S Rrna Cleavage) within 5.0Å range: probe atom residue distance (Å) B Occ d:Zn201 b:178.8 occ:1.00 SG d:CYS39 2.4 151.5 1.0 SG d:CYS21 2.4 150.0 1.0 SG d:CYS24 2.5 152.3 1.0 SG d:CYS42 2.5 153.6 1.0 CB d:CYS42 2.9 153.6 1.0 CB d:CYS24 3.2 152.3 1.0 N d:CYS24 3.5 152.3 1.0 CB d:CYS39 3.6 151.5 1.0 CB d:CYS21 3.6 150.0 1.0 CB d:VAL23 3.8 150.0 1.0 CA d:CYS24 3.9 152.3 1.0 N d:CYS39 3.9 151.5 1.0 CA d:CYS42 4.2 153.6 1.0 N d:CYS42 4.2 153.6 1.0 CA d:CYS39 4.3 151.5 1.0 C d:VAL23 4.3 150.0 1.0 CG1 d:VAL23 4.4 150.0 1.0 CA d:VAL23 4.5 150.0 1.0 N d:VAL23 4.6 150.0 1.0 CG2 d:VAL23 4.7 150.0 1.0 C d:CYS24 4.8 152.3 1.0 O d:CYS39 4.9 151.5 1.0 C d:CYS39 5.0 151.5 1.0 CA d:CYS21 5.0 150.0 1.0

Zinc binding site 2 out of 3 in the Human RIO1(Kd)-Stha Late Pre-40S Particle, Structural State A (Pre 18S Rrna Cleavage)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human RIO1(Kd)-Stha Late Pre-40S Particle, Structural State A (Pre 18S Rrna Cleavage) within 5.0Å range: probe atom residue distance (Å) B Occ f:Zn201 b:248.8 occ:1.00 SG f:CYS144 2.4 218.0 1.0 CB f:CYS141 2.5 218.9 1.0 CB f:LEU146 2.6 217.8 1.0 SG f:CYS141 2.7 218.9 1.0 SG f:CYS121 2.9 228.3 1.0 N f:LEU146 3.2 217.8 1.0 OG f:SER123 3.3 226.0 1.0 CA f:LEU146 3.4 217.8 1.0 CG f:LEU146 3.8 217.8 1.0 CD2 f:LEU146 3.8 217.8 1.0 CA f:CYS141 3.9 218.9 1.0 CB f:CYS144 3.9 218.0 1.0 N f:CYS144 4.0 218.0 1.0 N f:CYS145 4.0 216.2 1.0 C f:CYS144 4.1 218.0 1.0 SG f:CYS126 4.2 226.9 1.0 O f:LEU146 4.2 217.8 1.0 C f:CYS145 4.2 216.2 1.0 CA f:CYS144 4.2 218.0 1.0 C f:LEU146 4.2 217.8 1.0 C f:CYS141 4.3 218.9 1.0 CB f:CYS121 4.4 228.3 1.0 N f:CYS141 4.6 218.9 1.0 CB f:SER123 4.6 226.0 1.0 O f:CYS141 4.6 218.9 1.0 CA f:CYS145 4.6 216.2 1.0 O f:CYS144 4.7 218.0 1.0 CD1 f:LEU146 4.8 217.8 1.0 N f:GLY142 5.0 213.9 1.0

Zinc binding site 3 out of 3 in the Human RIO1(Kd)-Stha Late Pre-40S Particle, Structural State A (Pre 18S Rrna Cleavage)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Human RIO1(Kd)-Stha Late Pre-40S Particle, Structural State A (Pre 18S Rrna Cleavage) within 5.0Å range: probe atom residue distance (Å) B Occ y:Zn500 b:220.9 occ:1.00 SG y:CYS288 2.4 190.1 1.0 SG y:CYS270 2.4 207.1 1.0 CB y:CYS270 2.5 207.1 1.0 SG y:CYS273 2.5 201.1 1.0 SG y:CYS285 3.0 197.3 1.0 CB y:CYS285 3.3 197.3 1.0 CB y:CYS288 3.6 190.1 1.0 N y:CYS273 3.7 201.1 1.0 CA y:CYS270 3.8 207.1 1.0 CB y:CYS273 3.8 201.1 1.0 N y:CYS288 3.9 190.1 1.0 CG2 y:THR292 4.1 194.6 1.0 CA y:CYS273 4.3 201.1 1.0 CA y:CYS288 4.3 190.1 1.0 C y:CYS270 4.6 207.1 1.0 N y:GLY272 4.6 194.9 1.0 C y:GLY272 4.6 194.9 1.0 CA y:CYS285 4.7 197.3 1.0 CA y:GLY272 4.7 194.9 1.0 N y:CYS270 4.8 207.1 1.0 C y:CYS273 4.9 201.1 1.0 N y:GLY289 4.9 188.0 1.0 C y:CYS288 4.9 190.1 1.0 CB y:LYS275 4.9 207.7 1.0 CB y:HIS287 4.9 187.5 1.0 N y:PHE274 5.0 205.6 1.0

L.Plassart, R.Shayan, C.Montellese, D.Rinaldi, N.Larburu, C.Pichereaux, C.Froment, S.Lebaron, M.F.O'donohue, U.Kutay, J.Marcoux, P.E.Gleizes, C.Plisson-Chastang. The Final Step of 40S Ribosomal Subunit Maturation Is Controlled By A Dual Key Lock. Elife V. 10 2021.
ISSN: ESSN 2050-084X
PubMed: 33908345
DOI: 10.7554/ELIFE.61254