Zinc in PDB 7oim: Mouse RNF213, with Mixed Nucleotides Bound

All present enzymatic activity of Mouse RNF213, with Mixed Nucleotides Bound:
2.3.2.27;

The structure of Mouse RNF213, with Mixed Nucleotides Bound also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Zinc atom in the Mouse RNF213, with Mixed Nucleotides Bound (pdb code 7oim). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Mouse RNF213, with Mixed Nucleotides Bound, PDB code: 7oim:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Mouse RNF213, with Mixed Nucleotides Bound


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Mouse RNF213, with Mixed Nucleotides Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn5203 b:200.7 occ:1.00 CE1 A:HIS3964 1.6 152.1 1.0 ND1 A:HIS3964 2.1 152.1 1.0 SG A:CYS3985 2.3 156.0 1.0 SG A:CYS3962 2.3 156.3 1.0 SG A:CYS3982 2.3 148.1 1.0 NE2 A:HIS3964 2.6 152.1 1.0 CG A:HIS3964 3.2 152.1 1.0 CD2 A:HIS3964 3.4 152.1 1.0 CB A:CYS3982 3.5 148.1 1.0 CB A:CYS3985 3.5 156.0 1.0 CB A:CYS3962 3.5 156.3 1.0 N A:CYS3985 3.7 156.0 1.0 CA A:CYS3985 4.1 156.0 1.0 CD2 A:LEU3960 4.3 146.1 1.0 O A:CYS3962 4.4 156.3 1.0 CB A:HIS3964 4.4 152.1 1.0 CB A:TYR3984 4.4 155.4 1.0 OG1 A:THR3987 4.6 143.9 1.0 C A:CYS3985 4.6 156.0 1.0 CB A:THR3987 4.6 143.9 1.0 C A:TYR3984 4.7 155.4 1.0 CA A:CYS3962 4.8 156.3 1.0 N A:LEU3986 4.8 145.1 1.0 CD2 A:TYR3984 4.8 155.4 1.0 N A:TYR3984 4.8 155.4 1.0 C A:CYS3962 4.9 156.3 1.0 CA A:CYS3982 4.9 148.1 1.0 CA A:TYR3984 4.9 155.4 1.0 N A:THR3987 4.9 143.9 1.0

Zinc binding site 2 out of 2 in the Mouse RNF213, with Mixed Nucleotides Bound


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Mouse RNF213, with Mixed Nucleotides Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn5204 b:175.1 occ:1.00 CB A:CYS3947 2.0 126.2 1.0 SG A:CYS3950 2.3 126.7 1.0 SG A:CYS3967 2.3 139.4 1.0 SG A:CYS3947 2.3 126.2 1.0 CB A:CYS3967 3.1 139.4 1.0 N A:CYS3967 3.3 139.4 1.0 CB A:CYS3950 3.4 126.7 1.0 CA A:CYS3947 3.4 126.2 1.0 SG A:CYS3970 3.6 139.8 1.0 N A:CYS3950 3.8 126.7 1.0 CA A:CYS3967 3.8 139.4 1.0 N A:CYS3947 4.0 126.2 1.0 C A:CYS3947 4.0 126.2 1.0 CB A:CYS3970 4.1 139.8 1.0 CA A:CYS3950 4.2 126.7 1.0 O A:CYS3947 4.2 126.2 1.0 O A:GLY3952 4.3 120.3 1.0 C A:TYR3966 4.4 134.0 1.0 CA A:TYR3966 4.7 134.0 1.0 N A:ILE3949 4.8 123.8 1.0 CB A:ILE3949 4.9 123.8 1.0 C A:CYS3950 4.9 126.7 1.0 N A:PHE3948 4.9 118.4 1.0 C A:ILE3949 4.9 123.8 1.0 N A:HIS3951 4.9 122.4 1.0

J.Ahel, A.J.Fletcher, D.Grabarczyk, E.Roitinger, L.Deszcz, A.Lehner, S.Virdee, T.Clausen. E3 Ubiquitin Ligase RNF213 Employs A Non-Canonical Zinc Finger Active Site and Is Allosterically Regulated By Atp To Be Published.