Chlorine in PDB 5unn: Crystal Structure of Nadph-Dependent Glyoxylate/Hydroxypyruvate Reductase SMC02828 (Smghra) From Sinorhizobium Meliloti in Apo Form

The structure of Crystal Structure of Nadph-Dependent Glyoxylate/Hydroxypyruvate Reductase SMC02828 (Smghra) From Sinorhizobium Meliloti in Apo Form, PDB code: 5unn was solved by I.G.Shabalin, C.Larowe, J.Kutner, O.A.Gasiorowska, K.B.Handing, J.Bonanno, S.C.Almo, W.Minor, New York Structural Genomics Research Consortium(Nysgrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.00
Space group	I 41
Cell size a, b, c (Å), α, β, γ (°)	128.592, 128.592, 122.847, 90.00, 90.00, 90.00
R / Rfree (%)	14.7 / 17.4

The binding sites of Chlorine atom in the Crystal Structure of Nadph-Dependent Glyoxylate/Hydroxypyruvate Reductase SMC02828 (Smghra) From Sinorhizobium Meliloti in Apo Form (pdb code 5unn). 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 Nadph-Dependent Glyoxylate/Hydroxypyruvate Reductase SMC02828 (Smghra) From Sinorhizobium Meliloti in Apo Form, PDB code: 5unn:

Chlorine binding site 1 out of 1 in the Crystal Structure of Nadph-Dependent Glyoxylate/Hydroxypyruvate Reductase SMC02828 (Smghra) From Sinorhizobium Meliloti in Apo Form


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 Nadph-Dependent Glyoxylate/Hydroxypyruvate Reductase SMC02828 (Smghra) From Sinorhizobium Meliloti in Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl402 b:36.2 occ:1.00 O A:HOH691 3.2 29.7 1.0 O A:HOH815 3.2 58.1 1.0 O A:HOH710 3.2 30.8 1.0 N A:ARG170 3.2 30.9 1.0 O A:HOH685 3.2 38.2 1.0 CA A:SER169 3.7 27.6 1.0 CD2 A:LEU200 3.8 25.8 1.0 CB A:SER169 3.8 28.9 1.0 C A:SER169 4.0 31.5 1.0 CB A:ARG170 4.0 34.1 1.0 CZ3 A:TRP168 4.1 28.2 1.0 CA A:ARG170 4.2 35.0 1.0 O A:HOH592 4.5 33.2 1.0 CH2 A:TRP168 4.6 27.2 1.0 CE3 A:TRP168 4.7 26.6 1.0 O A:HOH744 4.9 59.0 1.0 OG A:SER169 5.0 30.0 1.0

J.Kutner, I.G.Shabalin, D.Matelska, K.B.Handing, O.Gasiorowska, P.Sroka, M.W.Gorna, K.Ginalski, K.Wozniak, W.Minor. Structural, Biochemical, and Evolutionary Characterizations of Glyoxylate/Hydroxypyruvate Reductases Show Their Division Into Two Distinct Subfamilies. Biochemistry V. 57 963 2018.
ISSN: ISSN 1520-4995
PubMed: 29309127
DOI: 10.1021/ACS.BIOCHEM.7B01137