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Potassium in PDB 5h6g: Crystal Structure of A Thermostable Lipase From Marine Streptomyces

Protein crystallography data

The structure of Crystal Structure of A Thermostable Lipase From Marine Streptomyces, PDB code: 5h6g was solved by S.Hou, Z.Zhao, J.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 64.76 / 2.34
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 129.500, 129.500, 137.830, 90.00, 90.00, 120.00
R / Rfree (%) 19.1 / 22.2

Other elements in 5h6g:

The structure of Crystal Structure of A Thermostable Lipase From Marine Streptomyces also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of A Thermostable Lipase From Marine Streptomyces (pdb code 5h6g). 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 Crystal Structure of A Thermostable Lipase From Marine Streptomyces, PDB code: 5h6g:

Potassium binding site 1 out of 1 in 5h6g

Go back to Potassium Binding Sites List in 5h6g
Potassium binding site 1 out of 1 in the Crystal Structure of A Thermostable Lipase From Marine Streptomyces


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of A Thermostable Lipase From Marine Streptomyces within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K301

b:56.1
occ:1.00
OD1 B:ASP88 2.5 35.3 1.0
OD2 B:ASP92 2.6 34.8 1.0
CG B:ASP88 3.4 35.2 1.0
O B:HOH421 3.4 30.6 1.0
OD2 B:ASP88 3.5 38.3 1.0
CG B:ASP92 3.5 36.2 1.0
OD1 B:ASP92 3.5 38.5 1.0
O B:LEU122 4.3 35.4 1.0
O B:ASP88 4.5 31.9 1.0
CB B:ASP88 4.8 34.4 1.0
C B:ASP88 4.9 32.8 1.0
CB B:ASP92 4.9 34.9 1.0

Reference:

Z.Zhao, S.Hou, D.Lan, X.Wang, J.Liu, F.I.Khan, Y.Wang. Crystal Structure of A Lipase From Streptomyces Sp. Strain W007 - Implications For Thermostability and Regiospecificity Febs J. V. 284 3506 2017.
ISSN: ISSN 1742-4658
PubMed: 28857479
DOI: 10.1111/FEBS.14211
Page generated: Sat Aug 9 09:11:38 2025

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