Atomistry » Chlorine » PDB 5mgg-5mls » 5mlr
Atomistry »
  Chlorine »
    PDB 5mgg-5mls »
      5mlr »

Chlorine in PDB 5mlr: Plantago Major Multifunctional Oxidoreductase V150M Mutant in Complex with Citral and Nadp+

Enzymatic activity of Plantago Major Multifunctional Oxidoreductase V150M Mutant in Complex with Citral and Nadp+

All present enzymatic activity of Plantago Major Multifunctional Oxidoreductase V150M Mutant in Complex with Citral and Nadp+:
1.1.1.145;

Protein crystallography data

The structure of Plantago Major Multifunctional Oxidoreductase V150M Mutant in Complex with Citral and Nadp+, PDB code: 5mlr was solved by R.Fellows, C.M.Russo, S.G.Lee, J.M.Jez, J.D.Chisholm, C.Zubieta, M.Nanao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.20 / 1.46
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 79.510, 79.510, 137.613, 90.00, 90.00, 90.00
R / Rfree (%) 15.3 / 16.9

Other elements in 5mlr:

The structure of Plantago Major Multifunctional Oxidoreductase V150M Mutant in Complex with Citral and Nadp+ also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Plantago Major Multifunctional Oxidoreductase V150M Mutant in Complex with Citral and Nadp+ (pdb code 5mlr). 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 Plantago Major Multifunctional Oxidoreductase V150M Mutant in Complex with Citral and Nadp+, PDB code: 5mlr:

Chlorine binding site 1 out of 1 in 5mlr

Go back to Chlorine Binding Sites List in 5mlr
Chlorine binding site 1 out of 1 in the Plantago Major Multifunctional Oxidoreductase V150M Mutant in Complex with Citral and Nadp+


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Plantago Major Multifunctional Oxidoreductase V150M Mutant in Complex with Citral and Nadp+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl401

b:15.8
occ:1.00
 OH A:TYR179 3.0 16.7 1.0
NZ A:LYS147 3.1 19.3 1.0
N A:LYS147 3.3 13.7 1.0
O A:HOH901 3.3 21.9 1.0
N A:ARG146 3.4 13.8 1.0
CA A:GLY145 3.5 13.3 1.0
C6N A:NAP406 3.5 14.3 1.0
C A:GLY145 3.6 14.5 1.0
CG A:LYS147 3.6 16.2 1.0
CB A:LYS147 3.6 16.0 1.0
C5N A:NAP406 3.7 14.9 1.0
CE2 A:TYR179 3.8 15.4 1.0
CZ A:TYR179 3.8 16.8 1.0
CE A:LYS147 4.0 20.7 1.0
CA A:LYS147 4.0 14.5 1.0
O A:GRQ405 4.2 44.7 0.5
C7 A:GRQ404 4.2 20.9 0.5
C A:ARG146 4.2 14.2 1.0
O A:GLY145 4.3 15.0 1.0
CA A:ARG146 4.3 13.8 1.0
O A:GRQ404 4.3 14.2 0.5
CD A:LYS147 4.3 18.5 1.0
N A:GLY145 4.4 14.0 1.0
N1N A:NAP406 4.5 14.2 1.0
O A:HOH526 4.5 19.9 1.0
O2D A:NAP406 4.5 15.4 1.0
O A:PRO203 4.6 14.9 1.0
C4N A:NAP406 4.7 13.9 1.0
O A:THR144 4.8 15.8 1.0
O A:HOH592 4.8 18.1 1.0
C A:THR144 4.9 15.0 1.0
C6 A:GRQ405 4.9 34.2 0.5
C7 A:GRQ405 4.9 40.2 0.5
CB A:ARG146 4.9 13.9 1.0
C1D A:NAP406 4.9 14.3 1.0
CE A:MET215 4.9 14.3 0.7

Reference:

R.Fellows, C.M.Russo, C.S.Silva, S.G.Lee, J.M.Jez, J.D.Chisholm, C.Zubieta, M.H.Nanao. A Multisubstrate Reductase From Plantago Major: Structure-Function in the Short Chain Reductase Superfamily. Sci Rep V. 8 14796 2018.
ISSN: ESSN 2045-2322
PubMed: 30287897
DOI: 10.1038/S41598-018-32967-1
Page generated: Sat Jul 12 05:33:11 2025

Last articles

Fe in 2YXO
Fe in 2YRS
Fe in 2YXC
Fe in 2YNM
Fe in 2YVJ
Fe in 2YP1
Fe in 2YU2
Fe in 2YU1
Fe in 2YQB
Fe in 2YOO
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy