Chlorine in PDB 2vq7: Bacterial Flavin-Containing Monooxygenase in Complex with Nadp: Native Data

The structure of Bacterial Flavin-Containing Monooxygenase in Complex with Nadp: Native Data, PDB code: 2vq7 was solved by A.Alfieri, E.Malito, R.Orru, M.W.Fraaije, A.Mattevi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	188.98 / 2.60
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	219.589, 219.589, 133.610, 90.00, 90.00, 120.00
R / Rfree (%)	24.8 / 26.9

The binding sites of Chlorine atom in the Bacterial Flavin-Containing Monooxygenase in Complex with Nadp: Native Data (pdb code 2vq7). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Bacterial Flavin-Containing Monooxygenase in Complex with Nadp: Native Data, PDB code: 2vq7:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in the Bacterial Flavin-Containing Monooxygenase in Complex with Nadp: Native Data


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Bacterial Flavin-Containing Monooxygenase in Complex with Nadp: Native Data within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1453 b:58.0 occ:1.00 NH1 A:ARG24 3.7 51.6 1.0 NE2 A:GLN27 3.9 48.3 1.0 CE A:LYS118 4.1 56.9 1.0 NZ A:LYS118 4.4 58.2 1.0 CD A:LYS118 4.4 55.2 1.0 CG A:GLU31 4.6 51.4 1.0 OE1 A:GLN27 4.7 52.5 1.0 CD A:GLU31 4.7 55.6 1.0 NH2 A:ARG24 4.7 48.8 1.0 CZ A:ARG24 4.7 50.7 1.0 CD A:GLN27 4.7 49.2 1.0 CG A:LYS118 4.7 53.7 1.0 O A:HOH2002 4.7 41.1 1.0 OE2 A:GLU31 4.8 55.0 1.0 O A:LYS118 5.0 51.0 1.0

Chlorine binding site 2 out of 4 in the Bacterial Flavin-Containing Monooxygenase in Complex with Nadp: Native Data


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Bacterial Flavin-Containing Monooxygenase in Complex with Nadp: Native Data within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1454 b:58.9 occ:1.00 NH1 B:ARG24 3.7 51.6 1.0 CE B:LYS118 4.0 56.7 1.0 NE2 B:GLN27 4.0 48.4 1.0 O B:HOH2001 4.1 40.0 1.0 NZ B:LYS118 4.2 58.3 1.0 CD B:LYS118 4.4 54.9 1.0 NH2 B:ARG24 4.6 48.9 1.0 CZ B:ARG24 4.6 50.5 1.0 CG B:GLU31 4.7 51.4 1.0 CG B:LYS118 4.7 53.8 1.0 CD B:GLU31 4.8 55.6 1.0 OE1 B:GLN27 4.8 52.4 1.0 CD B:GLN27 4.8 49.2 1.0 OE2 B:GLU31 4.9 54.9 1.0

Chlorine binding site 3 out of 4 in the Bacterial Flavin-Containing Monooxygenase in Complex with Nadp: Native Data


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Bacterial Flavin-Containing Monooxygenase in Complex with Nadp: Native Data within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl1455 b:56.4 occ:1.00 NH1 C:ARG24 3.7 51.7 1.0 NE2 C:GLN27 3.8 48.4 1.0 CG C:GLU31 4.4 51.4 1.0 CE C:LYS118 4.4 56.8 1.0 O C:HOH2002 4.5 46.2 1.0 OE1 C:GLN27 4.5 52.4 1.0 CD C:GLU31 4.5 55.7 1.0 CD C:GLN27 4.6 49.4 1.0 NZ C:LYS118 4.7 58.3 1.0 CD C:LYS118 4.7 54.8 1.0 CZ C:ARG24 4.7 50.7 1.0 NH2 C:ARG24 4.7 49.0 1.0 OE2 C:GLU31 4.8 55.0 1.0 OE1 C:GLU31 5.0 57.5 1.0 CG C:LYS118 5.0 53.8 1.0

Chlorine binding site 4 out of 4 in the Bacterial Flavin-Containing Monooxygenase in Complex with Nadp: Native Data


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Bacterial Flavin-Containing Monooxygenase in Complex with Nadp: Native Data within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl1453 b:64.5 occ:1.00 NE2 D:GLN27 3.8 48.3 1.0 NH1 D:ARG24 3.8 51.6 1.0 CE D:LYS118 4.3 57.0 1.0 CG D:GLU31 4.4 51.4 1.0 CD D:GLU31 4.5 55.5 1.0 NZ D:LYS118 4.6 58.4 1.0 OE2 D:GLU31 4.6 54.9 1.0 OE1 D:GLN27 4.6 52.4 1.0 CD D:GLN27 4.7 49.2 1.0 CD D:LYS118 4.7 55.1 1.0 CZ D:ARG24 4.8 50.7 1.0 NH2 D:ARG24 4.8 49.2 1.0 OE1 D:GLU31 4.9 57.4 1.0 CG D:LYS118 4.9 53.7 1.0

A.Alfieri, E.Malito, R.Orru, M.W.Fraaije, A.Mattevi. Revealing the Moonlighting Role of Nadp in the Structure of A Flavin-Containing Monooxygenase. Proc.Nat.Acad.Sci.Usa V. 105 6572 2008.
ISSN: ISSN 0027-8424
PubMed: 18443301
DOI: 10.1073/PNAS.0800859105