Zinc in PDB 8w2u: Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament -Apo State (Consensus Map).

All present enzymatic activity of Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament -Apo State (Consensus Map).:
2.4.2.30;

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20;

Binding sites:

The binding sites of Zinc atom in the Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament -Apo State (Consensus Map). (pdb code 8w2u). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 20 binding sites of Zinc where determined in the Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament -Apo State (Consensus Map)., PDB code: 8w2u:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 20 in the Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament -Apo State (Consensus Map).


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 Tankyrase 2 Sam-Parp Filament -Apo State (Consensus Map). within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1201 b:136.4 occ:1.00 ND1 A:HIS1084 2.2 99.8 1.0 SG A:CYS1092 2.3 103.3 1.0 SG A:CYS1089 2.3 96.6 1.0 SG A:CYS1081 2.3 96.6 1.0 CE1 A:HIS1084 2.7 99.1 1.0 CB A:CYS1089 3.1 92.3 1.0 CG A:HIS1084 3.3 100.0 1.0 CB A:CYS1081 3.4 92.9 1.0 CB A:CYS1092 3.6 98.5 1.0 NE2 A:HIS1084 3.8 99.7 1.0 CB A:HIS1084 4.0 98.4 1.0 CD2 A:HIS1084 4.1 99.6 1.0 N A:HIS1084 4.1 98.0 1.0 N A:CYS1092 4.3 99.2 1.0 CB A:VAL1083 4.3 97.8 1.0 CA A:CYS1089 4.5 93.1 1.0 CA A:CYS1092 4.6 99.6 1.0 CA A:HIS1084 4.7 99.4 1.0 CA A:CYS1081 4.8 93.2 1.0 CG2 A:VAL1083 4.9 96.5 1.0 O A:ASP1086 4.9 90.4 1.0 C A:VAL1083 4.9 98.2 1.0 N A:VAL1083 4.9 98.8 1.0 CA A:VAL1083 5.0 99.3 1.0

Zinc binding site 2 out of 20 in the Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament -Apo State (Consensus Map).


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 Tankyrase 2 Sam-Parp Filament -Apo State (Consensus Map). within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1201 b:155.1 occ:1.00 ND1 B:HIS1084 2.1 95.4 1.0 SG B:CYS1081 2.3 89.8 1.0 SG B:CYS1092 2.3 93.9 1.0 SG B:CYS1089 2.3 93.3 1.0 CE1 B:HIS1084 2.9 93.5 1.0 CG B:HIS1084 3.1 93.3 1.0 CB B:CYS1089 3.2 89.8 1.0 CB B:CYS1081 3.3 84.8 1.0 CB B:HIS1084 3.6 92.0 1.0 CB B:CYS1092 3.6 90.4 1.0 NE2 B:HIS1084 4.1 92.5 1.0 N B:HIS1084 4.1 92.1 1.0 N B:CYS1092 4.1 92.1 1.0 CD2 B:HIS1084 4.2 92.5 1.0 CA B:HIS1084 4.4 92.4 1.0 CA B:CYS1092 4.4 91.6 1.0 CB B:ILE1091 4.6 94.1 1.0 CA B:CYS1089 4.6 89.3 1.0 CB B:VAL1083 4.7 90.9 1.0 CA B:CYS1081 4.7 86.1 1.0 C B:VAL1083 4.9 91.9 1.0 C B:ILE1091 5.0 92.8 1.0 N B:VAL1083 5.0 92.3 1.0

Zinc binding site 3 out of 20 in the Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament -Apo State (Consensus Map).


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament -Apo State (Consensus Map). within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn1201 b:151.8 occ:1.00 NE2 C:HIS1084 2.1 90.0 1.0 CD2 C:HIS1084 2.2 89.3 1.0 CE1 C:HIS1084 2.3 88.7 1.0 SG C:CYS1081 2.3 80.5 1.0 SG C:CYS1092 2.3 86.3 1.0 SG C:CYS1089 2.3 85.2 1.0 CG C:HIS1084 2.4 88.5 1.0 ND1 C:HIS1084 2.4 89.5 1.0 CB C:CYS1092 3.2 83.9 1.0 CB C:CYS1089 3.4 79.3 1.0 CB C:CYS1081 3.4 80.0 1.0 CB C:HIS1084 3.5 85.9 1.0 N C:HIS1084 4.0 87.4 1.0 N C:CYS1092 4.0 83.1 1.0 CA C:CYS1092 4.2 84.2 1.0 CA C:HIS1084 4.3 87.2 1.0 CB C:VAL1083 4.6 86.3 1.0 CA C:CYS1089 4.8 80.8 1.0 CA C:CYS1081 4.9 80.0 1.0 C C:VAL1083 4.9 84.5 1.0 C C:ILE1091 4.9 79.3 1.0 CB C:ILE1091 5.0 85.4 1.0

Zinc binding site 4 out of 20 in the Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament -Apo State (Consensus Map).


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament -Apo State (Consensus Map). within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn1201 b:136.2 occ:1.00 SG D:CYS1081 2.3 82.7 1.0 SG D:CYS1089 2.3 84.4 1.0 ND1 D:HIS1084 2.3 90.5 1.0 CE1 D:HIS1084 2.9 87.9 1.0 CB D:CYS1089 2.9 79.4 1.0 CB D:CYS1081 3.2 81.2 1.0 SG D:CYS1092 3.3 85.0 1.0 CB D:CYS1092 3.3 76.5 1.0 CG D:HIS1084 3.5 87.3 1.0 CB D:VAL1083 4.0 88.9 1.0 N D:CYS1092 4.1 77.1 1.0 CB D:HIS1084 4.1 86.0 1.0 NE2 D:HIS1084 4.1 88.2 1.0 N D:HIS1084 4.2 84.3 1.0 CA D:CYS1092 4.3 77.2 1.0 CA D:CYS1089 4.4 79.6 1.0 CD2 D:HIS1084 4.4 85.5 1.0 CA D:CYS1081 4.7 79.5 1.0 CG2 D:VAL1083 4.7 88.0 1.0 C D:VAL1083 4.7 86.1 1.0 CA D:VAL1083 4.7 88.1 1.0 CG1 D:VAL1083 4.7 86.5 1.0 N D:VAL1083 4.8 87.5 1.0 CA D:HIS1084 4.8 85.5 1.0 C D:ILE1091 4.9 82.6 1.0 N D:ILE1091 5.0 80.0 1.0

Zinc binding site 5 out of 20 in the Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament -Apo State (Consensus Map).


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament -Apo State (Consensus Map). within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn1201 b:139.0 occ:1.00 ND1 E:HIS1084 2.1 86.6 1.0 SG E:CYS1081 2.3 76.8 1.0 SG E:CYS1092 2.3 77.4 1.0 SG E:CYS1089 2.3 74.7 1.0 CE1 E:HIS1084 3.0 84.8 1.0 CG E:HIS1084 3.0 81.9 1.0 CB E:CYS1081 3.2 76.0 1.0 CB E:CYS1089 3.3 70.8 1.0 CB E:HIS1084 3.4 80.7 1.0 CB E:CYS1092 3.5 70.9 1.0 N E:HIS1084 3.7 80.8 1.0 N E:CYS1092 4.0 75.8 1.0 NE2 E:HIS1084 4.1 84.9 1.0 CD2 E:HIS1084 4.1 81.3 1.0 CA E:HIS1084 4.1 80.8 1.0 CA E:CYS1092 4.4 72.5 1.0 CB E:VAL1083 4.5 87.0 1.0 CA E:CYS1081 4.6 76.0 1.0 CB E:ILE1091 4.7 77.3 1.0 CA E:CYS1089 4.7 68.8 1.0 C E:VAL1083 4.8 83.9 1.0 C E:HIS1084 4.9 84.2 1.0 N E:VAL1083 5.0 84.9 1.0

Zinc binding site 6 out of 20 in the Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament -Apo State (Consensus Map).


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament -Apo State (Consensus Map). within 5.0Å range: probe atom residue distance (Å) B Occ F:Zn1201 b:132.5 occ:1.00 ND1 F:HIS1084 2.1 75.6 1.0 SG F:CYS1092 2.3 66.9 1.0 SG F:CYS1089 2.3 70.3 1.0 SG F:CYS1081 2.3 65.1 1.0 CE1 F:HIS1084 2.8 73.1 1.0 CB F:CYS1081 3.2 63.8 1.0 CG F:HIS1084 3.3 70.8 1.0 CB F:CYS1089 3.3 60.3 1.0 CB F:CYS1092 3.4 56.5 1.0 CB F:HIS1084 3.8 70.9 1.0 NE2 F:HIS1084 4.0 73.2 1.0 N F:CYS1092 4.1 57.2 1.0 N F:HIS1084 4.1 72.8 1.0 CD2 F:HIS1084 4.3 71.8 1.0 CA F:CYS1092 4.3 58.4 1.0 CB F:VAL1083 4.6 73.2 1.0 CA F:HIS1084 4.6 72.3 1.0 CA F:CYS1089 4.7 59.1 1.0 CA F:CYS1081 4.7 63.7 1.0

Zinc binding site 7 out of 20 in the Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament -Apo State (Consensus Map).


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament -Apo State (Consensus Map). within 5.0Å range: probe atom residue distance (Å) B Occ G:Zn1201 b:115.6 occ:1.00 ND1 G:HIS1084 2.1 81.0 1.0 SG G:CYS1089 2.3 62.2 1.0 SG G:CYS1081 2.3 69.4 1.0 SG G:CYS1092 2.3 74.3 1.0 CE1 G:HIS1084 2.6 77.4 1.0 CB G:CYS1081 3.1 72.0 1.0 CB G:CYS1089 3.2 60.0 1.0 CB G:CYS1092 3.3 61.5 1.0 CG G:HIS1084 3.4 76.5 1.0 NE2 G:HIS1084 3.9 76.8 1.0 N G:CYS1092 3.9 63.1 1.0 CB G:HIS1084 4.0 72.9 1.0 CA G:CYS1092 4.2 61.6 1.0 CD2 G:HIS1084 4.2 75.0 1.0 N G:HIS1084 4.3 76.5 1.0 CB G:ILE1091 4.5 64.9 1.0 CA G:CYS1081 4.5 70.7 1.0 CB G:VAL1083 4.6 74.8 1.0 CA G:CYS1089 4.7 62.0 1.0 CA G:HIS1084 4.8 74.4 1.0 OH G:TYR1073 4.9 55.0 1.0 C G:ILE1091 4.9 62.1 1.0 N G:VAL1083 5.0 76.0 1.0 N G:ILE1091 5.0 63.1 1.0

Zinc binding site 8 out of 20 in the Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament -Apo State (Consensus Map).


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament -Apo State (Consensus Map). within 5.0Å range: probe atom residue distance (Å) B Occ H:Zn1201 b:129.0 occ:1.00 ND1 H:HIS1084 2.1 83.0 1.0 SG H:CYS1081 2.3 76.0 1.0 SG H:CYS1092 2.3 71.6 1.0 SG H:CYS1089 2.3 72.9 1.0 CE1 H:HIS1084 3.0 78.8 1.0 CG H:HIS1084 3.1 82.1 1.0 CB H:CYS1081 3.1 73.5 1.0 CB H:CYS1089 3.2 66.0 1.0 CB H:HIS1084 3.4 77.9 1.0 CB H:CYS1092 3.5 64.0 1.0 N H:HIS1084 3.8 76.2 1.0 N H:CYS1092 4.0 65.6 1.0 NE2 H:HIS1084 4.2 81.7 1.0 CA H:HIS1084 4.2 76.2 1.0 CD2 H:HIS1084 4.2 81.7 1.0 CA H:CYS1092 4.3 64.9 1.0 CB H:VAL1083 4.5 78.7 1.0 CA H:CYS1081 4.6 74.5 1.0 CB H:ILE1091 4.7 68.0 1.0 CA H:CYS1089 4.7 67.9 1.0 C H:VAL1083 4.8 79.0 1.0 C H:HIS1084 4.9 77.8 1.0

Zinc binding site 9 out of 20 in the Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament -Apo State (Consensus Map).


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament -Apo State (Consensus Map). within 5.0Å range: probe atom residue distance (Å) B Occ I:Zn1201 b:144.1 occ:1.00 SG I:CYS1092 2.3 81.9 1.0 SG I:CYS1089 2.3 76.4 1.0 SG I:CYS1081 2.3 80.3 1.0 ND1 I:HIS1084 2.3 81.4 1.0 CG I:HIS1084 2.3 82.4 1.0 CE1 I:HIS1084 2.7 81.8 1.0 CD2 I:HIS1084 2.7 81.7 1.0 NE2 I:HIS1084 2.9 82.6 1.0 CB I:HIS1084 3.1 79.7 1.0 N I:HIS1084 3.5 80.5 1.0 CB I:CYS1089 3.5 74.6 1.0 CB I:CYS1092 3.6 72.8 1.0 CB I:CYS1081 3.6 74.3 1.0 CA I:HIS1084 3.9 78.3 1.0 C I:VAL1083 4.3 78.0 1.0 N I:CYS1092 4.3 76.1 1.0 CG1 I:VAL1083 4.5 78.0 1.0 CB I:VAL1083 4.5 79.2 1.0 CA I:CYS1092 4.5 75.5 1.0 CA I:VAL1083 4.7 79.7 1.0 N I:VAL1083 4.7 81.5 1.0 CB I:ILE1091 4.8 74.9 1.0 CA I:CYS1089 4.9 72.6 1.0 CA I:CYS1081 5.0 75.6 1.0 C I:HIS1084 5.0 80.6 1.0

Zinc binding site 10 out of 20 in the Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament -Apo State (Consensus Map).


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of Cryo-Em Structure of Human Tankyrase 2 Sam-Parp Filament -Apo State (Consensus Map). within 5.0Å range: probe atom residue distance (Å) B Occ J:Zn1201 b:127.6 occ:1.00 ND1 J:HIS1084 2.1 91.4 1.0 SG J:CYS1081 2.3 81.7 1.0 SG J:CYS1089 2.3 84.3 1.0 SG J:CYS1092 2.3 85.9 1.0 CE1 J:HIS1084 3.0 88.8 1.0 CB J:CYS1081 3.1 81.5 1.0 CG J:HIS1084 3.1 86.0 1.0 CB J:CYS1089 3.3 80.7 1.0 CB J:CYS1092 3.3 80.4 1.0 CB J:HIS1084 3.5 83.7 1.0 N J:HIS1084 3.9 86.5 1.0 N J:CYS1092 3.9 81.4 1.0 NE2 J:HIS1084 4.1 89.9 1.0 CD2 J:HIS1084 4.2 87.0 1.0 CA J:CYS1092 4.2 81.7 1.0 CA J:HIS1084 4.3 84.5 1.0 CA J:CYS1081 4.6 82.1 1.0 CA J:CYS1089 4.7 80.7 1.0 CB J:ILE1091 4.7 85.6 1.0 CB J:VAL1083 4.7 85.4 1.0 C J:ILE1091 4.9 82.7 1.0 C J:HIS1084 5.0 85.8 1.0

J.Zimmerman, B.F.Malone, E.Finkin-Groner, S.Sun, R.Liang, M.Foronda, E.M.Schatoff, E.Granowsky, S.Goswami, A.Katti, B.Leach, H.Alcorn, T.Tammela, Y.Fukase, T.Khan, D.J.Huggins, J.Ginn, N.Liverton, R.K.Hite, L.E.Dow. A Potent and Selective TNKS2 Inhibitor For Tumor-Selective Wnt Suppression. Biorxiv 2025.
ISSN: ISSN 2692-8205
PubMed: 40093088
DOI: 10.1101/2025.03.04.641305