Chlorine in PDB 4lgm: Crystal Structure of Sulfolobus Solfataricus VPS4

All present enzymatic activity of Crystal Structure of Sulfolobus Solfataricus VPS4:
3.6.4.6;

The structure of Crystal Structure of Sulfolobus Solfataricus VPS4, PDB code: 4lgm was solved by H.Han, C.P.Hill, F.G.Whitby, N.Monroe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	23.17 / 2.71
Space group	P 64
Cell size a, b, c (Å), α, β, γ (°)	101.321, 101.321, 64.743, 90.00, 90.00, 120.00
R / Rfree (%)	21.7 / 25.5

The binding sites of Chlorine atom in the Crystal Structure of Sulfolobus Solfataricus VPS4 (pdb code 4lgm). 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 Crystal Structure of Sulfolobus Solfataricus VPS4, PDB code: 4lgm:

Chlorine binding site 1 out of 1 in the Crystal Structure of Sulfolobus Solfataricus VPS4


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Sulfolobus Solfataricus VPS4 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl401 b:98.2 occ:1.00 NZ A:LYS147 2.4 75.3 1.0 CE A:LYS147 3.0 72.4 1.0 N A:CYS145 3.1 62.3 1.0 CG A:LYS147 3.2 71.2 1.0 O A:PRO142 3.2 77.2 1.0 CA A:CYS145 3.6 60.7 1.0 N A:GLY146 3.6 74.4 1.0 CD A:LYS147 3.6 71.2 1.0 N A:GLY144 3.7 76.4 1.0 CB A:CYS145 3.7 69.0 1.0 N A:LYS147 3.8 65.4 1.0 C A:CYS145 3.8 63.6 1.0 CB A:LYS147 3.8 59.2 1.0 CA A:PRO143 4.0 75.4 1.0 C A:PRO143 4.1 68.3 1.0 C A:PRO142 4.2 76.5 1.0 C A:GLY144 4.2 70.4 1.0 OD1 A:ASN251 4.3 95.3 1.0 CA A:LYS147 4.4 65.8 1.0 CA A:GLY144 4.5 67.3 1.0 N A:PRO143 4.6 83.2 1.0 O A:CYS145 4.7 67.0 1.0 CA A:GLY146 4.7 69.2 1.0 C A:GLY146 4.7 65.3 1.0 O A:GLY141 4.9 68.9 1.0 O A:PRO143 4.9 67.3 1.0

N.Monroe, H.Han, M.D.Gonciarz, D.M.Eckert, M.A.Karren, F.G.Whitby, W.I.Sundquist, C.P.Hill. The Oligomeric State of the Active VPS4 Aaa Atpase. J.Mol.Biol. V. 426 510 2014.
ISSN: ISSN 0022-2836
PubMed: 24161953
DOI: 10.1016/J.JMB.2013.09.043