Atomistry » Potassium » PDB 2hzv-2o84 » 2j0b
Atomistry »
  Potassium »
    PDB 2hzv-2o84 »
      2j0b »

Potassium in PDB 2j0b: Structure of the Catalytic Domain of Mouse Manic Fringe in Complex with Udp and Manganese

Enzymatic activity of Structure of the Catalytic Domain of Mouse Manic Fringe in Complex with Udp and Manganese

All present enzymatic activity of Structure of the Catalytic Domain of Mouse Manic Fringe in Complex with Udp and Manganese:
2.4.1.222;

Protein crystallography data

The structure of Structure of the Catalytic Domain of Mouse Manic Fringe in Complex with Udp and Manganese, PDB code: 2j0b was solved by M.Jinek, Y.-W.Chen, H.Clausen, S.M.Cohen, E.Conti, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 80.85 / 2.10
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 161.760, 40.970, 38.370, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 22.1

Other elements in 2j0b:

The structure of Structure of the Catalytic Domain of Mouse Manic Fringe in Complex with Udp and Manganese also contains other interesting chemical elements:

Manganese (Mn) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Structure of the Catalytic Domain of Mouse Manic Fringe in Complex with Udp and Manganese (pdb code 2j0b). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Structure of the Catalytic Domain of Mouse Manic Fringe in Complex with Udp and Manganese, PDB code: 2j0b:

Potassium binding site 1 out of 1 in 2j0b

Go back to Potassium Binding Sites List in 2j0b
Potassium binding site 1 out of 1 in the Structure of the Catalytic Domain of Mouse Manic Fringe in Complex with Udp and Manganese


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of the Catalytic Domain of Mouse Manic Fringe in Complex with Udp and Manganese within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K1320

b:35.8
occ:1.00
 O A:ALA118 2.4 34.8 1.0
O A:HOH2052 2.5 35.0 1.0
O A:LEU229 2.6 33.3 1.0
O A:LEU226 2.7 40.1 1.0
OG1 A:THR234 2.8 22.3 1.0
C A:ALA118 3.5 34.2 1.0
C A:LEU229 3.7 34.4 1.0
C A:LEU226 3.8 40.2 1.0
O A:ILE227 3.8 41.0 1.0
CB A:THR234 3.9 22.5 1.0
CG2 A:THR234 4.0 24.0 1.0
N A:LEU229 4.2 37.7 1.0
C A:ILE227 4.2 40.9 1.0
CA A:LEU229 4.3 35.9 1.0
CA A:ALA118 4.4 34.9 1.0
N A:LEU119 4.4 33.3 1.0
CA A:ILE227 4.4 40.9 1.0
O A:PRO230 4.4 29.4 1.0
CB A:LEU229 4.4 35.8 1.0
CA A:LEU119 4.4 33.2 1.0
N A:ILE227 4.5 40.7 1.0
C A:PRO230 4.6 30.5 1.0
CA A:LEU226 4.7 40.1 1.0
CB A:LEU226 4.8 39.8 1.0
OD1 A:ASP231 4.8 30.6 1.0
N A:PRO230 4.8 33.1 1.0
CA A:PRO230 5.0 31.9 1.0
N A:ALA118 5.0 35.1 1.0
N A:ASP231 5.0 29.4 1.0
CD1 A:LEU119 5.0 35.2 1.0

Reference:

M.Jinek, Y.-W.Chen, H.Clausen, S.M.Cohen, E.Conti. Structural Insights Into the Notch-Modifying Glycosyltransferase Fringe Nat.Struct.Mol.Biol. V. 13 945 2006.
ISSN: ISSN 1545-9993
PubMed: 16964258
DOI: 10.1038/NSMB1144
Page generated: Mon Aug 12 06:43:34 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy