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Potassium in PDB 4kgd: High-Resolution Crystal Structure of Pyruvate Oxidase From L. Plantarum in Complex with Phosphate

Enzymatic activity of High-Resolution Crystal Structure of Pyruvate Oxidase From L. Plantarum in Complex with Phosphate

All present enzymatic activity of High-Resolution Crystal Structure of Pyruvate Oxidase From L. Plantarum in Complex with Phosphate:
1.2.3.3;

Protein crystallography data

The structure of High-Resolution Crystal Structure of Pyruvate Oxidase From L. Plantarum in Complex with Phosphate, PDB code: 4kgd was solved by P.Neumann, K.Tittmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.06
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 119.280, 154.160, 165.470, 90.00, 90.00, 90.00
R / Rfree (%) 12.7 / 15.1

Other elements in 4kgd:

The structure of High-Resolution Crystal Structure of Pyruvate Oxidase From L. Plantarum in Complex with Phosphate also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the High-Resolution Crystal Structure of Pyruvate Oxidase From L. Plantarum in Complex with Phosphate (pdb code 4kgd). 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 High-Resolution Crystal Structure of Pyruvate Oxidase From L. Plantarum in Complex with Phosphate, PDB code: 4kgd:

Potassium binding site 1 out of 1 in 4kgd

Go back to Potassium Binding Sites List in 4kgd
Potassium binding site 1 out of 1 in the High-Resolution Crystal Structure of Pyruvate Oxidase From L. Plantarum in Complex with Phosphate


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of High-Resolution Crystal Structure of Pyruvate Oxidase From L. Plantarum in Complex with Phosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K709

b:7.1
occ:0.50
OE1 A:GLN455 2.7 7.4 1.0
O A:MET452 2.8 6.2 1.0
O A:HOH825 3.0 7.0 1.0
CD A:GLN455 3.6 7.1 1.0
C A:MET452 3.8 5.1 1.0
NE2 A:GLN455 4.0 7.1 1.0
CD2 A:HIS58 4.1 5.3 1.0
O A:SER451 4.5 4.3 0.4
O A:SER451 4.6 8.0 0.6
CA A:THR453 4.6 5.3 1.0
N A:THR453 4.6 5.2 1.0
CA A:MET452 4.7 5.2 1.0
CG A:GLN455 4.7 7.1 1.0
NE2 A:HIS58 4.8 5.8 1.0
CG A:HIS58 4.9 5.1 1.0

Reference:

D.Meyer, P.Neumann, R.Ficner, K.Tittmann. Observation of A Stable Carbene at the Active Site of A Thiamin Enzyme. Nat.Chem.Biol. V. 9 488 2013.
ISSN: ISSN 1552-4450
PubMed: 23748673
DOI: 10.1038/NCHEMBIO.1275
Page generated: Sun Dec 13 23:36:11 2020

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