Chlorine in PDB 6big: Crystal Structure of Cobalt-Substituted Synechocystis Aco

All present enzymatic activity of Crystal Structure of Cobalt-Substituted Synechocystis Aco:
1.13.11.75;

The structure of Crystal Structure of Cobalt-Substituted Synechocystis Aco, PDB code: 6big was solved by X.Sui, W.Shi, P.D.Kiser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.39 / 2.21
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	118.074, 124.531, 202.608, 90.00, 90.00, 90.00
R / Rfree (%)	20.8 / 22.9

The structure of Crystal Structure of Cobalt-Substituted Synechocystis Aco also contains other interesting chemical elements:

Cobalt

(Co)

4 atoms

The binding sites of Chlorine atom in the Crystal Structure of Cobalt-Substituted Synechocystis Aco (pdb code 6big). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of Cobalt-Substituted Synechocystis Aco, PDB code: 6big:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of Cobalt-Substituted Synechocystis Aco


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 Cobalt-Substituted Synechocystis Aco within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl502 b:61.7 occ:1.00 N C:ASP32 3.1 54.7 1.0 ND2 A:ASN338 3.4 60.3 1.0 ND2 A:ASN341 3.4 78.2 1.0 O A:HOH689 3.5 54.4 1.0 CA C:TRP31 3.6 50.7 1.0 O C:ASP32 3.7 59.7 1.0 CE3 C:TRP31 3.7 50.5 1.0 CB A:ASN338 3.8 57.4 1.0 C C:TRP31 3.9 52.0 1.0 CG A:ASN341 3.9 75.8 1.0 C C:ASP32 3.9 57.5 1.0 CA C:ASP32 4.0 56.4 1.0 CD1 C:TYR33 4.0 54.7 1.0 CG A:ASN338 4.1 58.3 1.0 CB C:TRP31 4.1 48.9 1.0 OD1 A:ASN341 4.2 79.6 1.0 CD2 C:TRP31 4.4 48.4 1.0 O C:GLU30 4.4 50.9 1.0 CZ3 C:TRP31 4.5 51.5 1.0 CG C:TRP31 4.6 47.8 1.0 CB C:ASP32 4.6 58.6 1.0 CB A:ASN341 4.7 70.0 1.0 CB C:TYR33 4.7 58.3 1.0 N C:TYR33 4.8 56.9 1.0 N C:TRP31 4.8 49.6 1.0 CG C:TYR33 4.8 56.3 1.0 CE1 C:TYR33 4.8 53.6 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of Cobalt-Substituted Synechocystis Aco


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of Cobalt-Substituted Synechocystis Aco within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl503 b:66.2 occ:1.00 N A:GLN153 3.2 40.2 1.0 ND2 A:ASN132 3.5 37.7 1.0 CA A:GLY152 3.8 39.3 1.0 CB A:GLN153 3.9 43.6 1.0 C A:GLY152 4.0 39.1 1.0 CG A:GLN153 4.1 45.9 1.0 CA A:GLY177 4.1 63.2 1.0 CA A:GLN153 4.1 40.6 1.0 CD2 A:LEU167 4.2 44.2 1.0 OE1 A:GLN153 4.3 51.4 1.0 O A:GLY177 4.4 62.3 1.0 CG A:ASN132 4.5 37.3 1.0 CD A:GLN153 4.6 48.8 1.0 C A:GLY177 4.6 62.5 1.0 CD1 A:LEU167 4.7 46.9 1.0 CB A:ASN132 4.7 38.6 1.0 O A:GLN153 4.7 36.9 1.0 O A:HOH792 4.8 54.0 1.0 N A:GLY177 4.9 64.4 1.0 C A:GLN153 4.9 38.4 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of Cobalt-Substituted Synechocystis Aco


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of Cobalt-Substituted Synechocystis Aco within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl502 b:58.8 occ:1.00 N D:ASP32 3.0 57.6 1.0 ND2 B:ASN341 3.1 73.9 1.0 ND2 B:ASN338 3.4 65.6 1.0 O D:ASP32 3.6 61.5 1.0 CA D:TRP31 3.6 52.4 1.0 CE3 D:TRP31 3.8 52.8 1.0 C D:TRP31 3.8 54.6 1.0 C D:ASP32 3.9 61.0 1.0 CA D:ASP32 4.0 59.7 1.0 CD2 D:TYR33 4.0 59.1 1.0 CB B:ASN338 4.1 62.4 1.0 CB D:TRP31 4.1 51.7 1.0 CG B:ASN341 4.1 72.8 1.0 CG B:ASN338 4.3 63.9 1.0 OD1 B:ASN341 4.3 77.6 1.0 O D:GLU30 4.4 51.5 1.0 CD2 D:TRP31 4.4 50.7 1.0 CB D:ASP32 4.5 60.9 1.0 CZ3 D:TRP31 4.6 53.5 1.0 CG D:TRP31 4.6 50.3 1.0 CB D:TYR33 4.7 63.1 1.0 N D:TYR33 4.7 61.5 1.0 CE2 D:TYR33 4.8 57.2 1.0 N D:TRP31 4.8 51.2 1.0 CG D:TYR33 4.8 61.3 1.0

X.Sui, E.R.Farquhar, H.E.Hill, J.Von Lintig, W.Shi, P.D.Kiser. Preparation and Characterization of Metal-Substituted Carotenoid Cleavage Oxygenases. J. Biol. Inorg. Chem. V. 23 887 2018.
ISSN: ESSN 1432-1327
PubMed: 29946976
DOI: 10.1007/S00775-018-1586-0