Chlorine in PDB 3lf2: Nadph Bound Structure of the Short Chain Oxidoreductase Q9HYA2 From Pseudomonas Aeruginosa PAO1 Containing An Atypical Catalytic Center

The structure of Nadph Bound Structure of the Short Chain Oxidoreductase Q9HYA2 From Pseudomonas Aeruginosa PAO1 Containing An Atypical Catalytic Center, PDB code: 3lf2 was solved by R.Huether, T.C.Umland, W.L.Duax, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.89 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	65.788, 112.607, 136.584, 90.00, 90.00, 90.00
R / Rfree (%)	17.3 / 23.8

The binding sites of Chlorine atom in the Nadph Bound Structure of the Short Chain Oxidoreductase Q9HYA2 From Pseudomonas Aeruginosa PAO1 Containing An Atypical Catalytic Center (pdb code 3lf2). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Nadph Bound Structure of the Short Chain Oxidoreductase Q9HYA2 From Pseudomonas Aeruginosa PAO1 Containing An Atypical Catalytic Center, PDB code: 3lf2:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Nadph Bound Structure of the Short Chain Oxidoreductase Q9HYA2 From Pseudomonas Aeruginosa PAO1 Containing An Atypical Catalytic Center


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Nadph Bound Structure of the Short Chain Oxidoreductase Q9HYA2 From Pseudomonas Aeruginosa PAO1 Containing An Atypical Catalytic Center within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl302 b:77.7 occ:1.00 NH2 A:ARG163 2.8 58.0 1.0 NE A:ARG163 3.5 47.1 1.0 CE A:MET156 3.6 42.0 1.0 CZ A:ARG163 3.6 53.5 1.0 CD1 A:LEU148 3.7 31.4 1.0 CG2 A:THR159 3.8 34.2 0.5 CB A:SER146 4.0 36.5 1.0 OG1 A:THR159 4.0 34.6 0.5 OG A:SER146 4.1 41.5 1.0 CA A:GLY98 4.2 70.0 1.0 CG A:LEU148 4.6 30.2 1.0 CG2 A:THR159 4.6 33.4 0.5 O A:HOH509 4.7 43.3 1.0 N A:GLY98 4.8 72.0 1.0 CD A:ARG163 4.9 38.2 1.0 NH1 A:ARG163 4.9 55.3 1.0 CB A:THR159 4.9 33.9 0.5 CB A:THR159 5.0 33.8 0.5

Chlorine binding site 2 out of 3 in the Nadph Bound Structure of the Short Chain Oxidoreductase Q9HYA2 From Pseudomonas Aeruginosa PAO1 Containing An Atypical Catalytic Center


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Nadph Bound Structure of the Short Chain Oxidoreductase Q9HYA2 From Pseudomonas Aeruginosa PAO1 Containing An Atypical Catalytic Center within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl302 b:0.1 occ:1.00 NE C:ARG163 2.9 55.1 1.0 NH2 C:ARG163 3.0 60.0 1.0 CZ C:ARG163 3.2 53.8 1.0 CD1 C:LEU148 3.7 26.6 1.0 CG2 C:THR159 3.7 38.4 0.5 OG1 C:THR159 3.8 38.8 0.5 CE C:MET156 3.8 40.1 1.0 CD C:ARG163 3.9 50.5 1.0 O C:HOH443 3.9 46.1 1.0 CB C:SER146 4.0 39.5 1.0 OG C:SER146 4.1 44.8 1.0 NH1 C:ARG163 4.3 48.5 1.0 CA C:GLY98 4.4 87.3 1.0 CG C:LEU148 4.8 28.8 1.0 CB C:THR159 4.9 38.4 0.5 CG2 C:THR159 4.9 38.4 0.5 CB C:THR159 4.9 38.1 0.5

Chlorine binding site 3 out of 3 in the Nadph Bound Structure of the Short Chain Oxidoreductase Q9HYA2 From Pseudomonas Aeruginosa PAO1 Containing An Atypical Catalytic Center


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Nadph Bound Structure of the Short Chain Oxidoreductase Q9HYA2 From Pseudomonas Aeruginosa PAO1 Containing An Atypical Catalytic Center within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl303 b:75.8 occ:1.00 NH2 D:ARG163 2.8 50.4 1.0 CD1 D:LEU148 3.5 33.0 1.0 CZ D:ARG163 3.5 46.2 1.0 OG D:SER146 3.6 34.6 1.0 NE D:ARG163 3.7 43.3 1.0 O D:HOH443 3.7 40.6 1.0 CB D:SER146 3.7 30.5 1.0 CE D:MET156 3.9 26.8 1.0 CG2 D:THR159 4.3 27.4 0.5 CA D:GLY98 4.4 87.2 1.0 OG1 D:THR159 4.5 27.7 0.5 CG D:LEU148 4.5 32.9 1.0 NH1 D:ARG163 4.6 44.6 1.0 N D:GLY98 4.8 93.4 1.0 CD D:ARG163 4.9 37.6 1.0

R.Huether, Q.Mao, W.L.Duax, T.C.Umland. The Short-Chain Oxidoreductase Q9HYA2 From Pseudomonas Aeruginosa PAO1 Contains An Atypical Catalytic Center. Protein Sci. V. 19 1097 2010.
ISSN: ISSN 0961-8368
PubMed: 20340135
DOI: 10.1002/PRO.384