Atomistry » Manganese » PDB 1ss9-1uvi » 1ss9
Atomistry »
  Manganese »
    PDB 1ss9-1uvi »
      1ss9 »

Manganese in PDB 1ss9: Crystal Structural Analysis of Active Site Mutant Q189E of Lgtc

Enzymatic activity of Crystal Structural Analysis of Active Site Mutant Q189E of Lgtc

All present enzymatic activity of Crystal Structural Analysis of Active Site Mutant Q189E of Lgtc:
2.4.1.44;

Protein crystallography data

The structure of Crystal Structural Analysis of Active Site Mutant Q189E of Lgtc, PDB code: 1ss9 was solved by L.L.Lairson, C.P.Chiu, H.D.Ly, S.He, W.W.Wakarchuk, N.C.Strynadka, S.G.Withers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.30 / 2.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 39.850, 75.934, 86.905, 90.00, 90.00, 90.00
R / Rfree (%) 21.7 / 28.3

Other elements in 1ss9:

The structure of Crystal Structural Analysis of Active Site Mutant Q189E of Lgtc also contains other interesting chemical elements:

Fluorine (F) 1 atom

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structural Analysis of Active Site Mutant Q189E of Lgtc (pdb code 1ss9). 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 Structural Analysis of Active Site Mutant Q189E of Lgtc, PDB code: 1ss9:

Manganese binding site 1 out of 1 in 1ss9

Go back to Manganese Binding Sites List in 1ss9
Manganese binding site 1 out of 1 in the Crystal Structural Analysis of Active Site Mutant Q189E of Lgtc


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structural Analysis of Active Site Mutant Q189E of Lgtc within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn400

b:7.1
occ:1.00
O1B A:UPF401 2.1 20.6 1.0
NE2 A:HIS244 2.2 6.5 1.0
O1A A:UPF401 2.3 18.4 1.0
OD1 A:ASP103 2.4 16.7 1.0
OD1 A:ASP105 2.5 11.0 1.0
OD2 A:ASP105 2.6 3.6 1.0
CG A:ASP105 2.8 8.7 1.0
CE1 A:HIS244 3.1 5.5 1.0
CG A:ASP103 3.2 14.3 1.0
CD2 A:HIS244 3.3 8.0 1.0
PA A:UPF401 3.3 13.1 1.0
PB A:UPF401 3.3 19.0 1.0
O3A A:UPF401 3.3 20.5 1.0
CB A:ASP103 3.4 7.8 1.0
C3' A:UPF401 3.9 39.8 1.0
O3' A:UPF401 4.0 38.1 1.0
O2B A:UPF401 4.1 19.6 1.0
ND1 A:HIS244 4.2 8.2 1.0
F2' A:UPF401 4.2 36.4 1.0
O5D A:UPF401 4.3 19.3 1.0
CB A:ASP105 4.3 9.6 1.0
CG A:HIS244 4.4 10.5 1.0
OD2 A:ASP103 4.4 17.9 1.0
O3B A:UPF401 4.4 27.9 1.0
O2A A:UPF401 4.4 22.8 1.0
NZ A:LYS250 4.4 0.7 1.0
O3D A:UPF401 4.5 13.9 1.0
C2' A:UPF401 4.7 37.5 1.0
CA A:CYS246 4.7 18.7 1.0
CA A:ASP103 4.8 7.3 1.0
C5D A:UPF401 4.9 14.5 1.0
N A:ASP105 4.9 8.6 1.0
CA A:GLY155 4.9 3.2 1.0

Reference:

L.L.Lairson, C.P.Chiu, H.D.Ly, S.He, W.W.Wakarchuk, N.C.Strynadka, S.G.Withers. Intermediate Trapping on A Mutant Retaining Alpha-Galactosyltransferase Identifies An Unexpected Aspartate Residue. J.Biol.Chem. V. 279 28339 2004.
ISSN: ISSN 0021-9258
PubMed: 15075344
DOI: 10.1074/JBC.M400451200
Page generated: Sat Oct 5 12:27:38 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