Zinc in PDB 5twf: Regulation of Protein Interactions By MOB1 Phosphorylation

The structure of Regulation of Protein Interactions By MOB1 Phosphorylation, PDB code: 5twf was solved by S.Xiong, F.Sicheri, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.40 / 3.14
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	86.132, 86.160, 138.081, 90.00, 90.00, 90.00
R / Rfree (%)	26.3 / 29.1

The binding sites of Zinc atom in the Regulation of Protein Interactions By MOB1 Phosphorylation (pdb code 5twf). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Regulation of Protein Interactions By MOB1 Phosphorylation, PDB code: 5twf:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Regulation of Protein Interactions By MOB1 Phosphorylation


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Regulation of Protein Interactions By MOB1 Phosphorylation within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:90.2 occ:1.00 NE2 A:HIS166 1.8 1.0 1.0 SG A:CYS84 2.1 0.6 1.0 NE2 A:HIS161 2.2 84.7 1.0 SG A:CYS79 2.6 99.7 1.0 CE1 A:HIS166 2.6 0.0 1.0 CE1 A:HIS161 2.7 77.4 1.0 CD2 A:HIS166 2.9 0.9 1.0 CB A:CYS79 3.3 98.7 1.0 CD2 A:HIS161 3.4 81.0 1.0 CA A:CYS79 3.6 98.9 1.0 ND1 A:HIS166 3.8 0.7 1.0 CB A:CYS84 3.8 1.0 1.0 OG A:SER83 3.9 0.6 1.0 ND1 A:HIS161 3.9 75.0 1.0 CG A:HIS166 3.9 0.7 1.0 OE1 A:GLN165 3.9 0.4 1.0 CG A:HIS161 4.2 80.7 1.0 O A:PHE78 4.6 0.8 1.0 N A:CYS79 4.6 98.3 1.0 C A:CYS79 4.7 99.3 1.0 CB A:ALA111 4.8 98.0 1.0 CA A:CYS84 4.8 0.6 1.0 CB A:GLN165 4.9 0.1 1.0 N A:CYS84 4.9 0.1 1.0 O A:SER83 4.9 0.4 1.0 N A:THR80 5.0 0.9 1.0 C A:PHE78 5.0 0.3 1.0 C A:SER83 5.0 0.7 1.0 CD A:GLN165 5.0 0.8 1.0

Zinc binding site 2 out of 2 in the Regulation of Protein Interactions By MOB1 Phosphorylation


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Regulation of Protein Interactions By MOB1 Phosphorylation within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn301 b:98.4 occ:1.00 CE1 B:HIS166 2.1 97.3 1.0 NE2 B:HIS161 2.1 80.3 1.0 SG B:CYS79 2.2 0.7 1.0 NE2 B:HIS166 2.4 99.8 1.0 SG B:CYS84 2.5 0.5 1.0 CB B:CYS84 2.6 0.2 1.0 CD2 B:HIS161 3.1 75.9 1.0 CE1 B:HIS161 3.1 82.6 1.0 CB B:CYS79 3.3 0.5 1.0 ND1 B:HIS166 3.3 97.0 1.0 CA B:CYS79 3.6 0.9 1.0 CD2 B:HIS166 3.7 0.9 1.0 CB B:ALA111 4.0 0.2 1.0 CA B:CYS84 4.1 0.5 1.0 CG B:HIS166 4.1 99.4 1.0 ND1 B:HIS161 4.2 79.9 1.0 CG B:HIS161 4.2 75.7 1.0 OG B:SER83 4.4 0.1 1.0 N B:CYS79 4.5 0.0 1.0 N B:CYS84 4.6 0.5 1.0 C B:CYS79 4.6 0.2 1.0 OH B:TYR72 4.7 71.2 1.0 N B:THR80 4.8 0.7 1.0 O B:PHE78 4.8 0.9 1.0 O B:CYS84 4.9 1.0 1.0 CD B:PRO112 5.0 0.0 1.0

S.Xiong, A.L.Couzens, M.J.Kean, D.Y.Mao, S.Guettler, I.Kurinov, A.C.Gingras, F.Sicheri. Regulation of Protein Interactions By Mps One Binder (MOB1) Phosphorylation. Mol. Cell Proteomics V. 16 1111 2017.
ISSN: ESSN 1535-9484
PubMed: 28373297
DOI: 10.1074/MCP.M117.068130