Chlorine in PDB 4xyl: Ca. Korarchaeum Cryptofilum ACD1 in Complex with Coenzyme A

The structure of Ca. Korarchaeum Cryptofilum ACD1 in Complex with Coenzyme A, PDB code: 4xyl was solved by R.H.-J.Weisse, A.J.Scheidig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	83.46 / 1.95
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	102.460, 112.180, 124.890, 90.00, 90.00, 90.00
R / Rfree (%)	20.6 / 24.6

The binding sites of Chlorine atom in the Ca. Korarchaeum Cryptofilum ACD1 in Complex with Coenzyme A (pdb code 4xyl). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Ca. Korarchaeum Cryptofilum ACD1 in Complex with Coenzyme A, PDB code: 4xyl:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Ca. Korarchaeum Cryptofilum ACD1 in Complex with Coenzyme A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Ca. Korarchaeum Cryptofilum ACD1 in Complex with Coenzyme A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl501 b:40.5 occ:1.00 H C:GLY309 2.3 30.4 1.0 H A:LEU163 2.6 27.5 1.0 HB2 A:SER160 2.9 32.2 1.0 H A:ALA162 3.0 35.5 1.0 HB3 A:ALA162 3.0 29.7 1.0 N C:GLY309 3.1 25.4 1.0 O A:HOH705 3.2 28.8 1.0 HA3 C:GLY307 3.2 39.7 1.0 HA3 C:GLY309 3.2 34.0 1.0 H A:GLY161 3.4 33.5 1.0 N A:LEU163 3.4 22.9 1.0 H C:GLY308 3.4 31.7 1.0 N A:ALA162 3.5 29.6 1.0 N C:GLY308 3.6 26.4 1.0 HB3 A:LEU163 3.6 30.5 1.0 CA C:GLY309 3.7 28.3 1.0 HB2 A:LEU163 3.7 30.5 1.0 C C:GLY307 3.7 31.0 1.0 CA C:GLY307 3.7 33.1 1.0 HA2 C:GLY307 3.7 39.7 1.0 CB A:SER160 3.8 26.8 1.0 H C:ALA310 3.8 28.0 1.0 CB A:ALA162 3.8 24.8 1.0 N A:GLY161 3.9 27.9 1.0 CB A:LEU163 4.0 25.4 1.0 HG A:SER160 4.0 44.0 1.0 CA A:ALA162 4.0 27.5 1.0 OG A:SER160 4.1 36.7 1.0 C C:GLY308 4.2 26.2 1.0 HB2 A:ALA162 4.2 29.7 1.0 C A:ALA162 4.2 25.5 1.0 CA A:LEU163 4.3 22.7 1.0 HA2 C:GLY309 4.4 34.0 1.0 C A:GLY161 4.4 28.3 1.0 CA C:GLY308 4.4 25.9 1.0 O C:GLY307 4.4 31.3 1.0 HA A:SER160 4.4 30.8 1.0 HG C:CYS382 4.4 35.6 1.0 HB3 A:SER160 4.4 32.2 1.0 N C:ALA310 4.5 23.3 1.0 CA A:SER160 4.5 25.6 1.0 C A:SER160 4.5 26.4 1.0 HB1 A:ALA162 4.6 29.7 1.0 HA3 C:GLY308 4.6 31.1 1.0 CA A:GLY161 4.6 25.2 1.0 C C:GLY309 4.6 24.0 1.0 H A:GLY164 4.7 31.5 1.0 HA3 A:GLY161 4.7 30.2 1.0 HA A:LEU163 4.9 27.3 1.0 HA A:ALA162 5.0 33.0 1.0

Chlorine binding site 2 out of 2 in the Ca. Korarchaeum Cryptofilum ACD1 in Complex with Coenzyme A


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Ca. Korarchaeum Cryptofilum ACD1 in Complex with Coenzyme A within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl501 b:40.0 occ:1.00 H A:GLY309 2.3 32.1 1.0 H C:LEU163 2.4 30.3 1.0 H C:ALA162 2.9 37.7 1.0 HB2 C:SER160 2.9 40.7 1.0 HB3 C:ALA162 3.1 36.7 1.0 N A:GLY309 3.1 26.7 1.0 HA3 A:GLY309 3.1 30.8 1.0 H C:GLY161 3.2 37.5 1.0 N C:LEU163 3.3 25.2 1.0 HA3 A:GLY307 3.4 38.1 1.0 HB3 C:LEU163 3.4 30.6 1.0 N C:ALA162 3.4 31.4 1.0 HB2 C:LEU163 3.5 30.6 1.0 H A:GLY308 3.5 36.3 1.0 CA A:GLY309 3.6 25.7 1.0 N A:GLY308 3.7 30.2 1.0 N C:GLY161 3.8 31.3 1.0 CB C:SER160 3.8 33.9 1.0 CB C:LEU163 3.8 25.5 1.0 H A:ALA310 3.9 34.3 1.0 CB C:ALA162 3.9 30.6 1.0 C A:GLY307 3.9 31.3 1.0 HA2 A:GLY307 3.9 38.1 1.0 CA A:GLY307 3.9 31.8 1.0 CA C:ALA162 4.0 29.8 1.0 C C:ALA162 4.1 24.2 1.0 OG C:SER160 4.2 41.5 1.0 CA C:LEU163 4.2 27.1 1.0 C A:GLY308 4.2 31.7 1.0 C C:GLY161 4.2 28.8 1.0 HB2 C:ALA162 4.2 36.7 1.0 HA C:SER160 4.3 37.0 1.0 HA2 A:GLY309 4.3 30.8 1.0 C C:SER160 4.4 31.7 1.0 CA A:GLY308 4.4 29.8 1.0 CA C:SER160 4.4 30.8 1.0 HG A:CYS382 4.4 33.8 1.0 CA C:GLY161 4.4 27.9 1.0 HB3 C:SER160 4.5 40.7 1.0 H C:GLY164 4.5 33.1 1.0 N A:ALA310 4.5 28.6 1.0 O A:GLY307 4.6 31.1 1.0 HB1 C:ALA162 4.6 36.7 1.0 HA3 A:GLY308 4.6 35.7 1.0 C A:GLY309 4.6 28.0 1.0 HA3 C:GLY161 4.6 33.5 1.0 HA C:LEU163 4.8 32.5 1.0 HA C:ALA162 4.9 35.8 1.0 HG C:SER160 5.0 49.8 1.0

R.H.Weie, A.Faust, M.Schmidt, P.Schonheit, A.J.Scheidig. Structure of Ndp-Forming Acetyl-Coa Synthetase ACD1 Reveals A Large Rearrangement For Phosphoryl Transfer. Proc.Natl.Acad.Sci.Usa V. 113 E519 2016.
ISSN: ESSN 1091-6490
PubMed: 26787904
DOI: 10.1073/PNAS.1518614113