Chlorine in PDB 2zys: A. Fulgidus Lipase with Fatty Acid Fragment and Chloride

All present enzymatic activity of A. Fulgidus Lipase with Fatty Acid Fragment and Chloride:
3.1.1.3;

The structure of A. Fulgidus Lipase with Fatty Acid Fragment and Chloride, PDB code: 2zys was solved by C.K.Chen, T.P.Ko, R.T.Guo, A.H.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 3.10
Space group	P 43
Cell size a, b, c (Å), α, β, γ (°)	99.552, 99.552, 59.021, 90.00, 90.00, 90.00
R / Rfree (%)	18.4 / 25.2

The binding sites of Chlorine atom in the A. Fulgidus Lipase with Fatty Acid Fragment and Chloride (pdb code 2zys). 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 A. Fulgidus Lipase with Fatty Acid Fragment and Chloride, PDB code: 2zys:

Chlorine binding site 1 out of 1 in the A. Fulgidus Lipase with Fatty Acid Fragment and Chloride


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of A. Fulgidus Lipase with Fatty Acid Fragment and Chloride within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl800 b:46.6 occ:1.00 CG2 A:VAL419 3.3 67.8 1.0 N A:VAL419 3.5 74.4 1.0 NE A:ARG420 3.7 53.9 1.0 NH2 A:ARG420 3.8 64.7 1.0 CG1 A:VAL418 3.9 66.6 1.0 CB A:VAL419 4.1 70.5 1.0 N A:ARG420 4.1 62.7 1.0 CA A:VAL419 4.2 70.3 1.0 CA A:VAL418 4.2 72.7 1.0 CZ A:ARG420 4.2 59.1 1.0 C A:VAL418 4.2 74.0 1.0 CG A:ARG420 4.5 55.4 1.0 NH1 A:ARG406 4.6 62.9 1.0 C A:VAL419 4.6 67.7 1.0 CD A:ARG420 4.7 48.2 1.0 NH2 A:ARG416 4.7 92.1 1.0 CB A:VAL418 4.7 68.9 1.0 CG A:ARG406 4.7 56.2 1.0 CB A:ARG420 4.9 57.4 1.0

C.K.Chen, G.C.Lee, T.P.Ko, R.T.Guo, L.M.Huang, H.J.Liu, Y.F.Ho, J.F.Shaw, A.H.Wang. Structure of the Alkalohyperthermophilic Archaeoglobus Fulgidus Lipase Contains A Unique C-Terminal Domain Essential For Long-Chain Substrate Binding. J.Mol.Biol. V. 390 672 2009.
ISSN: ISSN 0022-2836
PubMed: 19447113
DOI: 10.1016/J.JMB.2009.05.017