Chlorine in PDB 4ou8: Crystal Structure of Apocarotenoid Oxygenase in the Presence of C8E6

All present enzymatic activity of Crystal Structure of Apocarotenoid Oxygenase in the Presence of C8E6:
1.13.11.75;

The structure of Crystal Structure of Apocarotenoid Oxygenase in the Presence of C8E6, PDB code: 4ou8 was solved by X.Sui, W.Shi, K.Palczewski, P.D.Kiser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.58 / 2.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	118.561, 125.122, 203.012, 90.00, 90.00, 90.00
R / Rfree (%)	21.1 / 23.6

The structure of Crystal Structure of Apocarotenoid Oxygenase in the Presence of C8E6 also contains other interesting chemical elements:

Iron

(Fe)

4 atoms

The binding sites of Chlorine atom in the Crystal Structure of Apocarotenoid Oxygenase in the Presence of C8E6 (pdb code 4ou8). 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 Apocarotenoid Oxygenase in the Presence of C8E6, PDB code: 4ou8:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Crystal Structure of Apocarotenoid Oxygenase in the Presence of C8E6


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 Apocarotenoid Oxygenase in the Presence of C8E6 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl502 b:50.4 occ:1.00 ND2 A:ASN341 3.0 54.9 1.0 N C:ASP32 3.1 47.3 1.0 ND2 A:ASN338 3.6 53.0 1.0 O C:ASP32 3.6 52.1 1.0 CA C:TRP31 3.7 44.2 1.0 CE3 C:TRP31 3.8 44.6 1.0 C C:ASP32 3.9 50.1 1.0 C C:TRP31 3.9 45.5 1.0 CD2 C:TYR33 4.0 45.7 1.0 CB A:ASN338 4.0 50.5 1.0 CG A:ASN341 4.1 54.1 1.0 CA C:ASP32 4.1 48.2 1.0 CB C:TRP31 4.1 42.3 1.0 CG A:ASN338 4.3 50.9 1.0 OD1 A:ASN341 4.3 57.0 1.0 CB C:TYR33 4.4 50.5 1.0 CD2 C:TRP31 4.6 42.5 1.0 N C:TYR33 4.6 49.8 1.0 CG C:TYR33 4.6 47.9 1.0 CB C:ASP32 4.7 49.1 1.0 O C:GLU30 4.7 44.6 1.0 CZ3 C:TRP31 4.7 45.3 1.0 CG C:TRP31 4.7 41.3 1.0 CE2 C:TYR33 4.9 43.6 1.0 N C:TRP31 5.0 43.8 1.0

Chlorine binding site 2 out of 3 in the Crystal Structure of Apocarotenoid Oxygenase in the Presence of C8E6


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 Apocarotenoid Oxygenase in the Presence of C8E6 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl502 b:58.2 occ:1.00 ND2 B:ASN132 3.2 32.5 1.0 N B:GLN153 3.3 34.1 1.0 CA B:GLY152 3.9 35.2 1.0 CB B:GLN153 4.1 34.9 1.0 C B:GLY152 4.1 33.7 1.0 CB B:ASN132 4.2 33.4 1.0 CG B:ASN132 4.2 32.3 1.0 CA B:GLN153 4.2 33.9 1.0 CD2 B:LEU167 4.3 33.0 1.0 CG B:GLN153 4.4 36.0 1.0 CD1 B:LEU167 4.5 35.3 1.0 CA B:GLY177 4.5 68.5 1.0 O B:GLN153 4.6 33.2 1.0 OE1 B:GLN153 4.6 38.9 1.0 O B:GLY177 4.7 65.7 1.0 C B:GLN153 4.9 33.0 1.0 C B:GLY177 4.9 63.2 1.0 CD B:GLN153 4.9 37.3 1.0

Chlorine binding site 3 out of 3 in the Crystal Structure of Apocarotenoid Oxygenase in the Presence of C8E6


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 Apocarotenoid Oxygenase in the Presence of C8E6 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl503 b:57.2 occ:1.00 N D:ASP32 3.1 53.5 1.0 ND2 B:ASN341 3.4 55.2 1.0 ND2 B:ASN338 3.5 54.2 1.0 CA D:TRP31 3.7 49.7 1.0 O D:ASP32 3.7 58.4 1.0 CE3 D:TRP31 3.7 53.2 1.0 C D:TRP31 3.9 50.7 1.0 C D:ASP32 3.9 56.4 1.0 CD2 D:TYR33 4.0 51.3 1.0 CB D:TRP31 4.1 48.9 1.0 CA D:ASP32 4.1 55.3 1.0 CB B:ASN338 4.1 52.1 1.0 CG B:ASN338 4.3 52.9 1.0 CD2 D:TRP31 4.4 50.3 1.0 CG B:ASN341 4.5 54.6 1.0 CB D:TYR33 4.6 56.4 1.0 O D:GLU30 4.6 47.5 1.0 CG D:TRP31 4.6 48.3 1.0 CZ3 D:TRP31 4.6 54.6 1.0 CB D:ASP32 4.7 56.5 1.0 N D:TYR33 4.7 55.7 1.0 OD1 B:ASN341 4.7 56.9 1.0 CG D:TYR33 4.8 53.9 1.0 N D:TRP31 4.9 48.2 1.0 CE2 D:TYR33 4.9 49.3 1.0

X.Sui, P.D.Kiser, T.Che, P.R.Carey, M.Golczak, W.Shi, J.Von Lintig, K.Palczewski. Analysis of Carotenoid Isomerase Activity in A Prototypical Carotenoid Cleavage Enzyme, Apocarotenoid Oxygenase (Aco). J.Biol.Chem. V. 289 12286 2014.
ISSN: ISSN 0021-9258
PubMed: 24648526
DOI: 10.1074/JBC.M114.552836