Chlorine in PDB 4if5: Structure of Human MEC17

All present enzymatic activity of Structure of Human MEC17:
2.3.1.108;

The structure of Structure of Human MEC17, PDB code: 4if5 was solved by A.M.Davenport, L.Collins, P.Minor, P.Sternberg, A.Hoelz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 1.70
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	41.747, 122.297, 37.541, 90.00, 90.00, 90.00
R / Rfree (%)	17.8 / 21.4

The binding sites of Chlorine atom in the Structure of Human MEC17 (pdb code 4if5). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Structure of Human MEC17, PDB code: 4if5:

Chlorine binding site 1 out of 1 in the Structure of Human MEC17


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Human MEC17 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl202 b:29.8 occ:1.00 NZ A:LYS98 3.2 22.4 1.0 ND1 A:HIS75 3.4 30.0 1.0 N A:MSE70 3.5 26.6 1.0 CB A:ARG69 3.5 27.1 1.0 N A:SER66 3.5 24.2 1.0 O A:SER66 3.5 25.9 1.0 CD A:LYS98 3.6 22.8 1.0 CA A:THR65 3.7 22.2 1.0 C A:ARG69 3.7 25.7 1.0 CG A:MSE70 3.7 30.7 1.0 SE A:MSE70 3.9 36.5 1.0 CE A:LYS98 3.9 21.2 1.0 CA A:MSE70 4.0 29.2 1.0 CG2 A:THR65 4.0 20.9 1.0 O A:ILE64 4.0 24.9 1.0 C A:THR65 4.1 24.8 1.0 CE1 A:HIS75 4.1 29.6 1.0 CA A:ARG69 4.1 23.8 1.0 O A:ARG69 4.2 31.8 1.0 CB A:THR65 4.2 21.7 1.0 CB A:MSE70 4.4 29.6 1.0 OG1 A:THR65 4.4 24.1 1.0 C A:SER66 4.4 21.5 1.0 CG A:HIS75 4.5 30.5 1.0 NE A:ARG69 4.5 39.6 1.0 CA A:SER66 4.6 25.5 1.0 N A:THR65 4.7 20.1 1.0 CB A:HIS75 4.8 22.4 1.0 CG A:ARG69 4.8 36.6 1.0 C A:ILE64 4.8 26.3 1.0 N A:ARG69 4.8 28.4 1.0 CD A:ARG69 4.9 42.7 1.0 CG A:LYS98 5.0 20.7 1.0

A.M.Davenport, L.N.Collins, H.Chiu, P.J.Minor, P.W.Sternberg, A.Hoelz. Structural and Functional Characterization of the Alpha-Tubulin Acetyltransferase Mec-17. J.Mol.Biol. V. 426 2605 2014.
ISSN: ISSN 0022-2836
PubMed: 24846647
DOI: 10.1016/J.JMB.2014.05.009