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Potassium in PDB 5xnr: Truncated Alyq with CBM32 and Alginate Lyase Domains

Protein crystallography data

The structure of Truncated Alyq with CBM32 and Alginate Lyase Domains, PDB code: 5xnr was solved by A.H.Teh, P.F.Sim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.19 / 2.30
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 74.317, 74.317, 179.733, 90.00, 90.00, 90.00
R / Rfree (%) 22.6 / 27.5

Other elements in 5xnr:

The structure of Truncated Alyq with CBM32 and Alginate Lyase Domains also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Truncated Alyq with CBM32 and Alginate Lyase Domains (pdb code 5xnr). 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 Truncated Alyq with CBM32 and Alginate Lyase Domains, PDB code: 5xnr:

Potassium binding site 1 out of 1 in 5xnr

Go back to Potassium Binding Sites List in 5xnr
Potassium binding site 1 out of 1 in the Truncated Alyq with CBM32 and Alginate Lyase Domains


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Truncated Alyq with CBM32 and Alginate Lyase Domains within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K602

b:52.5
occ:1.00
O A:THR353 2.6 41.8 1.0
OE2 A:GLU357 2.6 41.6 1.0
OD1 A:ASP351 2.6 39.5 1.0
OG1 A:THR353 2.6 29.1 1.0
OD2 A:ASP351 2.9 42.3 1.0
CG A:ASP351 3.1 39.9 1.0
CD A:GLU357 3.3 37.8 1.0
C A:THR353 3.6 36.9 1.0
CB A:THR353 3.7 36.4 1.0
O A:HOH704 3.8 32.6 1.0
CG A:GLU357 3.8 36.6 1.0
CA A:THR353 4.1 36.3 1.0
OE1 A:GLU357 4.2 42.4 1.0
N A:THR353 4.4 33.6 1.0
CB A:ASP351 4.6 39.8 1.0
N A:LEU354 4.7 37.5 1.0

Reference:

P.F.Sim, G.Furusawa, A.H.Teh. Functional and Structural Studies of A Multidomain Alginate Lyase From Persicobacter Sp. Ccb-QB2. Sci Rep V. 7 13656 2017.
ISSN: ESSN 2045-2322
PubMed: 29057942
DOI: 10.1038/S41598-017-13288-1
Page generated: Mon Aug 12 15:09:24 2024

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