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Potassium in PDB 4tkx: Structure of Protease

Enzymatic activity of Structure of Protease

All present enzymatic activity of Structure of Protease:
3.4.22.47;

Protein crystallography data

The structure of Structure of Protease, PDB code: 4tkx was solved by M.A.Gorman, M.W.Parker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.71 / 1.60
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 116.941, 116.941, 86.852, 90.00, 90.00, 90.00
R / Rfree (%) 12 / 14.5

Other elements in 4tkx:

The structure of Structure of Protease also contains other interesting chemical elements:

Lead (Pb) 1 atom
Sodium (Na) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Structure of Protease (pdb code 4tkx). 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 Protease, PDB code: 4tkx:

Potassium binding site 1 out of 1 in 4tkx

Go back to Potassium Binding Sites List in 4tkx
Potassium binding site 1 out of 1 in the Structure of Protease


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of Protease within 5.0Å range:
probe atom residue distance (Å) B Occ
L:K707

b:25.2
occ:0.28
OD2 L:ASP388 2.5 20.5 1.0
O L:HOH805 2.6 23.8 1.0
HD1 L:TRP391 3.0 27.3 1.0
HE2 L:HIS444 3.1 23.0 1.0
HE1 L:HIS444 3.1 24.3 1.0
CG L:ASP388 3.5 20.1 1.0
NE2 L:HIS444 3.7 19.1 1.0
CE1 L:HIS444 3.7 20.3 1.0
CD1 L:TRP391 3.8 22.8 1.0
OD1 L:ASP388 3.8 20.7 1.0
HE1 L:TRP513 3.9 23.6 1.0
HE1 L:TRP391 3.9 28.1 1.0
NE1 L:TRP391 4.2 23.4 1.0
O L:HOH880 4.5 41.2 0.5
O2S L:TCK720 4.5 24.8 1.0
NE1 L:TRP513 4.6 19.6 1.0
HZ2 L:TRP513 4.7 21.9 1.0
CB L:ASP388 4.9 19.1 1.0
HB2 L:ASP388 5.0 22.9 1.0
HB2 L:TRP391 5.0 25.8 1.0
ND1 L:HIS444 5.0 20.1 1.0

Reference:

M.A.Gorman, C.A.Seers, B.J.Michell, S.C.Feil, N.L.Huq, K.J.Cross, E.C.Reynolds, M.W.Parker. Structure of the Lysine Specific Protease Kgp From Porphyromonas Gingivalis, A Target For Improved Oral Health. Protein Sci. V. 24 162 2015.
ISSN: ESSN 1469-896X
PubMed: 25327141
DOI: 10.1002/PRO.2589
Page generated: Mon Aug 12 12:05:00 2024

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