Zinc in PDB 8soj: Cryo-Em Structure of Human Cst Bound to POT1(Esdl)/TPP1 in the Absence of Telomeric Ssdna

All present enzymatic activity of Cryo-Em Structure of Human Cst Bound to POT1(Esdl)/TPP1 in the Absence of Telomeric Ssdna:
2.7.7.48; 3.4.22.28; 3.4.22.29; 3.6.1.15;

The binding sites of Zinc atom in the Cryo-Em Structure of Human Cst Bound to POT1(Esdl)/TPP1 in the Absence of Telomeric Ssdna (pdb code 8soj). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Cryo-Em Structure of Human Cst Bound to POT1(Esdl)/TPP1 in the Absence of Telomeric Ssdna, PDB code: 8soj:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Cryo-Em Structure of Human Cst Bound to POT1(Esdl)/TPP1 in the Absence of Telomeric Ssdna


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Cryo-Em Structure of Human Cst Bound to POT1(Esdl)/TPP1 in the Absence of Telomeric Ssdna within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1301 b:156.1 occ:1.00 SG A:CYS1055 2.3 99.3 1.0 SG A:CYS1043 2.3 77.7 1.0 SG A:CYS1062 2.3 110.0 1.0 SG A:CYS1046 2.3 94.2 1.0 HG A:CYS1055 2.5 99.3 1.0 HG A:CYS1046 2.7 94.2 1.0 HB3 A:CYS1043 2.8 77.7 1.0 HB2 A:CYS1062 3.0 110.0 1.0 CB A:CYS1043 3.0 77.7 1.0 HB2 A:CYS1043 3.1 77.7 1.0 CB A:CYS1062 3.2 110.0 1.0 HG A:CYS1043 3.3 77.7 1.0 HB2 A:ARG1057 3.3 107.4 1.0 HG A:CYS1062 3.4 110.0 1.0 HB2 A:CYS1055 3.6 99.3 1.0 CB A:CYS1055 3.7 99.3 1.0 HB3 A:CYS1062 3.7 110.0 1.0 HB2 A:TYR1045 3.8 78.6 1.0 HB3 A:CYS1055 4.0 99.3 1.0 CB A:CYS1046 4.0 94.2 1.0 H A:CYS1046 4.1 94.2 1.0 CB A:ARG1057 4.2 107.4 1.0 H A:ARG1057 4.2 107.4 1.0 HB3 A:ARG1057 4.2 107.4 1.0 HB3 A:CYS1046 4.2 94.2 1.0 H A:TYR1045 4.3 78.6 1.0 HD1 A:TYR1045 4.3 78.6 1.0 HA A:LEU1058 4.4 110.1 1.0 HA A:GLN1065 4.4 99.5 1.0 N A:CYS1046 4.4 94.2 1.0 CA A:CYS1043 4.5 77.7 1.0 O A:THR1064 4.5 99.7 1.0 HA A:CYS1062 4.5 110.0 1.0 CA A:CYS1062 4.5 110.0 1.0 HB2 A:CYS1046 4.6 94.2 1.0 C A:ARG1057 4.7 107.4 1.0 N A:LEU1058 4.7 110.1 1.0 O A:CYS1046 4.7 94.2 1.0 CB A:TYR1045 4.7 78.6 1.0 CA A:CYS1046 4.8 94.2 1.0 CA A:ARG1057 4.8 107.4 1.0 H A:LEU1058 4.8 110.1 1.0 HA A:CYS1043 4.8 77.7 1.0 N A:ARG1057 4.9 107.4 1.0 HA A:CYS1055 4.9 99.3 1.0 CA A:CYS1055 4.9 99.3 1.0 C A:CYS1043 4.9 77.7 1.0 N A:TYR1045 4.9 78.6 1.0 C A:TYR1045 5.0 78.6 1.0

Zinc binding site 2 out of 2 in the Cryo-Em Structure of Human Cst Bound to POT1(Esdl)/TPP1 in the Absence of Telomeric Ssdna


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Cryo-Em Structure of Human Cst Bound to POT1(Esdl)/TPP1 in the Absence of Telomeric Ssdna within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn701 b:168.3 occ:1.00 SG D:CYS382 2.3 103.0 1.0 SG D:CYS506 2.3 119.8 1.0 SG D:CYS385 2.3 108.7 1.0 SG D:CYS503 2.3 116.5 1.0 HG D:CYS503 3.0 116.5 1.0 HG D:CYS382 3.1 103.0 1.0 HG D:CYS385 3.2 108.7 1.0 HG D:CYS506 3.2 119.8 1.0 HB3 D:CYS503 3.3 116.5 1.0 CB D:CYS503 3.3 116.5 1.0 HB3 D:CYS382 3.3 103.0 1.0 HB2 D:CYS503 3.4 116.5 1.0 CB D:CYS382 3.4 103.0 1.0 H D:CYS385 3.4 108.7 1.0 HB3 D:LYS384 3.5 109.9 1.0 HB2 D:CYS506 3.5 119.8 1.0 HB3 D:CYS385 3.5 108.7 1.0 HB2 D:CYS382 3.5 103.0 1.0 CB D:CYS385 3.6 108.7 1.0 CB D:CYS506 3.6 119.8 1.0 H D:CYS506 3.6 119.8 1.0 HB3 D:GLN505 3.7 118.7 1.0 N D:CYS385 4.0 108.7 1.0 N D:CYS506 4.2 119.8 1.0 HB3 D:CYS506 4.3 119.8 1.0 HB3 D:LEU387 4.3 97.5 1.0 HB2 D:CYS385 4.3 108.7 1.0 CA D:CYS385 4.4 108.7 1.0 CB D:LYS384 4.4 109.9 1.0 H D:LYS384 4.5 109.9 1.0 CA D:CYS506 4.5 119.8 1.0 HD22 D:LEU387 4.7 97.5 1.0 HG12 D:VAL536 4.7 113.3 1.0 CB D:GLN505 4.7 118.7 1.0 CA D:CYS503 4.8 116.5 1.0 C D:LYS384 4.8 109.9 1.0 CA D:CYS382 4.8 103.0 1.0 HB2 D:LYS384 4.8 109.9 1.0 H D:GLN505 4.9 118.7 1.0 HG2 D:GLN505 4.9 118.7 1.0 HA D:CYS506 5.0 119.8 1.0 CA D:LYS384 5.0 109.9 1.0

S.W.Cai, H.Takai, T.Walz, T.De Lange. Structural Basis of Cst-Pol Alpha /Primase Recruitment and Regulation By POT1 at Telomeres. Biorxiv 2023.
ISSN: ISSN 2692-8205
PubMed: 37215005
DOI: 10.1101/2023.05.08.539880