Chlorine in PDB 4cw4: Crystal Structure of the Noncanonical Ketosynthase Faby From P. Aeruginosa

The structure of Crystal Structure of the Noncanonical Ketosynthase Faby From P. Aeruginosa, PDB code: 4cw4 was solved by H.S.T Bukhari, R.P.Jakob, T.Maier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.685 / 1.35
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	99.370, 123.310, 100.620, 90.00, 90.00, 90.00
R / Rfree (%)	14.76 / 17.7

The binding sites of Chlorine atom in the Crystal Structure of the Noncanonical Ketosynthase Faby From P. Aeruginosa (pdb code 4cw4). 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 the Noncanonical Ketosynthase Faby From P. Aeruginosa, PDB code: 4cw4:

Chlorine binding site 1 out of 1 in the Crystal Structure of the Noncanonical Ketosynthase Faby From P. Aeruginosa


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 the Noncanonical Ketosynthase Faby From P. Aeruginosa within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1636 b:10.3 occ:1.00 H A:SER437 2.5 11.6 1.0 HD21 A:ASN441 2.5 12.4 1.0 H A:PHE350 2.5 12.4 1.0 HA A:PRO349 2.9 11.9 1.0 HB3 A:ARG442 2.9 12.0 1.0 H A:THR438 3.0 13.9 1.0 HA A:SER437 3.1 11.3 1.0 HB3 A:ASN441 3.1 12.9 1.0 HD22 A:ASN353 3.1 13.2 1.0 N A:SER437 3.2 9.7 1.0 HA2 A:GLY435 3.3 9.3 1.0 ND2 A:ASN441 3.3 10.3 1.0 N A:PHE350 3.3 10.4 1.0 HA A:ARG442 3.4 11.6 1.0 H A:SER436 3.5 11.4 1.0 CA A:SER437 3.6 9.4 1.0 H A:ARG442 3.6 11.2 1.0 N A:THR438 3.6 11.6 1.0 N A:ARG442 3.6 9.3 1.0 HD21 A:ASN353 3.6 13.2 1.0 ND2 A:ASN353 3.7 11.0 1.0 CB A:ARG442 3.7 10.0 1.0 CA A:PRO349 3.7 9.9 1.0 CA A:ARG442 3.8 9.6 1.0 O A:THR438 3.8 12.6 1.0 HD22 A:ASN441 3.8 12.4 1.0 N A:SER436 3.8 9.5 1.0 HB3 A:PRO349 3.8 11.6 1.0 CB A:ASN441 4.0 10.8 1.0 HA A:PHE350 4.0 12.3 1.0 HB2 A:ARG442 4.0 12.0 1.0 C A:PRO349 4.0 10.0 1.0 C A:GLY435 4.1 9.8 1.0 CA A:GLY435 4.1 7.8 1.0 C A:SER437 4.1 9.9 1.0 CG A:ASN441 4.1 10.9 1.0 C A:ASN441 4.2 9.7 1.0 CA A:PHE350 4.3 10.2 1.0 C A:SER436 4.3 9.0 1.0 CB A:PRO349 4.3 9.6 1.0 CD1 A:PHE350 4.6 11.1 1.0 CG A:PHE350 4.6 10.2 1.0 HA3 A:GLY435 4.6 9.3 1.0 CA A:SER436 4.6 9.0 1.0 C A:THR438 4.6 12.3 1.0 CE1 A:PHE350 4.7 10.9 1.0 HB2 A:ASN441 4.7 12.9 1.0 CA A:ASN441 4.7 10.0 1.0 CA A:THR438 4.7 12.2 1.0 OG A:SER436 4.7 12.2 1.0 O A:GLY435 4.7 10.0 1.0 CD2 A:PHE350 4.7 11.1 1.0 O A:ASN441 4.8 10.9 1.0 HD1 A:PHE350 4.8 13.4 1.0 CZ A:PHE350 4.8 11.3 1.0 CE2 A:PHE350 4.9 11.7 1.0 N A:PRO349 4.9 9.7 1.0 CG A:ASN353 4.9 10.6 1.0 O A:ARG348 4.9 10.2 1.0 CG A:ARG442 4.9 10.3 1.0 HB2 A:PRO349 4.9 11.6 1.0 CB A:SER437 5.0 9.5 1.0 HD3 A:ARG442 5.0 13.7 1.0

H.S.Bukhari, R.P.Jakob, T.Maier. Evolutionary Origins of the Multienzyme Architecture of Giant Fungal Fatty Acid Synthase. Structure V. 22 1775 2014.
ISSN: ISSN 0969-2126
PubMed: 25456814
DOI: 10.1016/J.STR.2014.09.016