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Potassium in PDB 4wak: H. Influenzae Beta-Carbonic Anhydrase Variant W39V/G41A

Enzymatic activity of H. Influenzae Beta-Carbonic Anhydrase Variant W39V/G41A

All present enzymatic activity of H. Influenzae Beta-Carbonic Anhydrase Variant W39V/G41A:
4.2.1.1;

Protein crystallography data

The structure of H. Influenzae Beta-Carbonic Anhydrase Variant W39V/G41A, PDB code: 4wak was solved by K.M.Hoffmann, R.S.Rowlett, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.50 / 2.49
Space group I 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 48.330, 144.671, 129.010, 90.00, 90.00, 90.00
R / Rfree (%) 18.5 / 25.4

Other elements in 4wak:

The structure of H. Influenzae Beta-Carbonic Anhydrase Variant W39V/G41A also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the H. Influenzae Beta-Carbonic Anhydrase Variant W39V/G41A (pdb code 4wak). 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 H. Influenzae Beta-Carbonic Anhydrase Variant W39V/G41A, PDB code: 4wak:

Potassium binding site 1 out of 1 in 4wak

Go back to Potassium Binding Sites List in 4wak
Potassium binding site 1 out of 1 in the H. Influenzae Beta-Carbonic Anhydrase Variant W39V/G41A


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of H. Influenzae Beta-Carbonic Anhydrase Variant W39V/G41A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K303

b:62.1
occ:1.00
OD1 A:ASP74 3.2 17.8 1.0
N A:PHE75 3.7 18.3 1.0
CB A:PHE75 4.2 22.1 1.0
CA A:ASP74 4.3 16.9 1.0
CG A:ASP74 4.3 17.2 1.0
C A:ASP74 4.4 17.2 1.0
N A:ASN76 4.5 18.7 1.0
CA A:PHE75 4.5 19.8 1.0
O A:THR73 4.7 15.5 1.0
CB A:ASP74 4.7 16.8 1.0

Reference:

K.M.Hoffmann, H.R.Million-Perez, R.Merkhofer, H.Nicholson, R.S.Rowlett. Allosteric Reversion of Haemophilus Influenzae Beta-Carbonic Anhydrase Via A Proline Shift. Biochemistry V. 54 598 2015.
ISSN: ISSN 0006-2960
PubMed: 25506786
DOI: 10.1021/BI501116E
Page generated: Sun Dec 13 23:50:10 2020

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