Atomistry » Manganese » PDB 3uag-3vnm » 3uxi
Atomistry »
  Manganese »
    PDB 3uag-3vnm »
      3uxi »

Manganese in PDB 3uxi: Crystal Structure of L-Rhamnose Isomerase W38A Mutant From Bacillus Halodurans

Enzymatic activity of Crystal Structure of L-Rhamnose Isomerase W38A Mutant From Bacillus Halodurans

All present enzymatic activity of Crystal Structure of L-Rhamnose Isomerase W38A Mutant From Bacillus Halodurans:
5.3.1.14;

Protein crystallography data

The structure of Crystal Structure of L-Rhamnose Isomerase W38A Mutant From Bacillus Halodurans, PDB code: 3uxi was solved by T.T.N.Doan, P.Prabhu, J.K.Kim, M.Jeya, L.W.Kang, J.K.Lee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.87 / 2.73
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 83.380, 164.794, 92.837, 90.00, 117.02, 90.00
R / Rfree (%) 18.6 / 26.7

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of L-Rhamnose Isomerase W38A Mutant From Bacillus Halodurans (pdb code 3uxi). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of L-Rhamnose Isomerase W38A Mutant From Bacillus Halodurans, PDB code: 3uxi:

Manganese binding site 1 out of 1 in 3uxi

Go back to Manganese Binding Sites List in 3uxi
Manganese binding site 1 out of 1 in the Crystal Structure of L-Rhamnose Isomerase W38A Mutant From Bacillus Halodurans


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of L-Rhamnose Isomerase W38A Mutant From Bacillus Halodurans within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn419

b:83.3
occ:1.00
OE2 A:GLU225 2.5 31.1 1.0
OD2 A:ASP325 2.8 39.3 1.0
O A:HOH462 2.8 18.0 1.0
OD2 A:ASP258 2.9 30.5 1.0
NE2 A:HIS261 3.4 23.6 1.0
O A:HOH463 3.5 17.0 1.0
CG A:ASP325 3.5 34.3 1.0
CD A:GLU225 3.6 28.4 1.0
CE1 A:HIS261 3.7 23.7 1.0
OD1 A:ASP325 3.9 35.0 1.0
CG A:ASP258 3.9 23.9 1.0
OE1 A:GLU225 4.0 28.2 1.0
ND1 A:HIS285 4.1 28.6 1.0
OD1 A:ASP258 4.5 21.1 1.0
CD2 A:HIS261 4.6 21.9 1.0
OD2 A:ASP293 4.6 37.1 1.0
CB A:ASP325 4.6 32.6 1.0
CB A:ASP258 4.7 22.2 1.0
ND1 A:HIS261 4.8 22.6 1.0
CG A:GLU225 4.9 26.6 1.0
CE1 A:HIS285 4.9 29.8 1.0

Reference:

P.Prabhu, T.N.Doan, M.Tiwari, R.Singh, S.C.Kim, M.K.Hong, Y.C.Kang, L.W.Kang, J.K.Lee. Structure-Based Studies on the Metal Binding of Two-Metal-Dependent Sugar Isomerases. Febs J. V. 281 3446 2014.
ISSN: ISSN 1742-464X
PubMed: 24925069
DOI: 10.1111/FEBS.12872
Page generated: Sat Oct 5 18:14:51 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy