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Potassium in PDB 1t2n: Structure of A Thermostable Triple Mutant of Bacillus Subtilis Lipase Obtained Through Directed Evolution

Enzymatic activity of Structure of A Thermostable Triple Mutant of Bacillus Subtilis Lipase Obtained Through Directed Evolution

All present enzymatic activity of Structure of A Thermostable Triple Mutant of Bacillus Subtilis Lipase Obtained Through Directed Evolution:
3.1.1.3;

Protein crystallography data

The structure of Structure of A Thermostable Triple Mutant of Bacillus Subtilis Lipase Obtained Through Directed Evolution, PDB code: 1t2n was solved by E.Rajakumara, R.Sankaranarayanan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.14 / 1.80
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 75.863, 75.863, 102.680, 90.00, 90.00, 120.00
R / Rfree (%) 22.6 / 25.9

Potassium Binding Sites:

The binding sites of Potassium atom in the Structure of A Thermostable Triple Mutant of Bacillus Subtilis Lipase Obtained Through Directed Evolution (pdb code 1t2n). 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 A Thermostable Triple Mutant of Bacillus Subtilis Lipase Obtained Through Directed Evolution, PDB code: 1t2n:

Potassium binding site 1 out of 1 in 1t2n

Go back to Potassium Binding Sites List in 1t2n
Potassium binding site 1 out of 1 in the Structure of A Thermostable Triple Mutant of Bacillus Subtilis Lipase Obtained Through Directed Evolution


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of A Thermostable Triple Mutant of Bacillus Subtilis Lipase Obtained Through Directed Evolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K374

b:18.2
occ:1.00
 N A:HIS156 3.2 12.6 1.0
N A:MET134 3.3 16.6 1.0
O A:HOH539 3.7 37.6 1.0
CB A:HIS156 3.8 13.6 1.0
CB A:MET134 3.8 18.4 1.0
CA A:GLY155 3.9 12.5 1.0
CA A:MET134 4.0 17.7 1.0
C A:GLY155 4.0 12.9 1.0
CA A:HIS156 4.1 12.1 1.0
O A:ASP132 4.2 20.3 1.0
CG1 A:ILE135 4.2 15.9 1.0
CG A:MET134 4.2 22.1 1.0
C A:ASP133 4.2 18.6 1.0
N A:ILE135 4.3 15.1 1.0
CA A:ASP133 4.3 19.5 1.0
C A:MET134 4.4 18.0 1.0
OD1 A:ASP133 4.4 15.5 1.0
CD1 A:ILE135 4.6 14.7 1.0
CB A:ILE135 5.0 14.0 1.0

Reference:

P.Acharya, E.Rajakumara, R.Sankaranarayanan, N.M.Rao. Structural Basis of Selection and Thermostability of Laboratory Evolved Bacillus Subtilis Lipase. J.Mol.Biol. V. 341 1271 2004.
ISSN: ISSN 0022-2836
PubMed: 15321721
DOI: 10.1016/J.JMB.2004.06.059
Page generated: Mon Aug 12 05:23:07 2024

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