Chlorine in PDB 1s7f: Riml- Ribosomal L7/L12 Alpha-N-Protein Acetyltransferase Crystal Form I (Apo)

The structure of Riml- Ribosomal L7/L12 Alpha-N-Protein Acetyltransferase Crystal Form I (Apo), PDB code: 1s7f was solved by M.W.Vetting, L.P.De Carvalho, S.L.Roderick, J.S.Blanchard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.00
Space group	P 43 2 2
Cell size a, b, c (Å), α, β, γ (°)	68.400, 68.400, 89.600, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 24.2

The binding sites of Chlorine atom in the Riml- Ribosomal L7/L12 Alpha-N-Protein Acetyltransferase Crystal Form I (Apo) (pdb code 1s7f). 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 Riml- Ribosomal L7/L12 Alpha-N-Protein Acetyltransferase Crystal Form I (Apo), PDB code: 1s7f:

Chlorine binding site 1 out of 1 in the Riml- Ribosomal L7/L12 Alpha-N-Protein Acetyltransferase Crystal Form I (Apo)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Riml- Ribosomal L7/L12 Alpha-N-Protein Acetyltransferase Crystal Form I (Apo) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl998 b:38.9 occ:1.00 O A:HOH1029 3.2 32.7 1.0 N A:ARG135 3.3 25.7 1.0 ND2 A:ASN138 3.3 32.1 1.0 N A:LEU39 3.5 40.2 1.0 CB A:ARG135 3.6 27.6 1.0 CG A:LEU39 3.7 45.6 1.0 CG A:ARG135 3.8 31.7 1.0 CB A:SER38 3.9 39.9 1.0 CA A:SER38 4.0 40.3 1.0 CB A:ASN138 4.0 32.0 1.0 CA A:CYS134 4.0 26.8 1.0 CB A:LEU39 4.0 43.6 1.0 CD1 A:LEU39 4.0 45.7 1.0 CB A:CYS134 4.0 26.1 1.0 CA A:ARG135 4.1 26.5 1.0 C A:CYS134 4.1 24.9 1.0 CG A:ASN138 4.2 32.7 1.0 C A:SER38 4.3 39.8 1.0 CA A:LEU39 4.3 42.4 1.0 OD2 A:ASP40 4.7 42.4 1.0 CD A:ARG135 4.8 37.2 1.0 O A:GLN37 4.9 39.9 1.0 NE A:ARG135 5.0 41.7 1.0

M.W.Vetting, L.P.De Carvalho, S.L.Roderick, J.S.Blanchard. A Novel Dimeric Structure of the Riml Nalpha-Acetyltransferase From Salmonella Typhimurium. J.Biol.Chem. V. 280 22108 2005.
ISSN: ISSN 0021-9258
PubMed: 15817456
DOI: 10.1074/JBC.M502401200