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Potassium in PDB 5jdt: Structure of Spin-Labelled T4 Lysozyme Mutant L118C-R1 at 100K

Enzymatic activity of Structure of Spin-Labelled T4 Lysozyme Mutant L118C-R1 at 100K

All present enzymatic activity of Structure of Spin-Labelled T4 Lysozyme Mutant L118C-R1 at 100K:
3.2.1.17;

Protein crystallography data

The structure of Structure of Spin-Labelled T4 Lysozyme Mutant L118C-R1 at 100K, PDB code: 5jdt was solved by B.Loll, P.Consentius, U.Gohlke, R.Mueller, M.Kaupp, U.Heinemann, M.C.Wahl, T.Risse, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 17.76 / 1.00
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 60.280, 60.280, 96.970, 90.00, 90.00, 120.00
R / Rfree (%) 11.5 / 13

Other elements in 5jdt:

The structure of Structure of Spin-Labelled T4 Lysozyme Mutant L118C-R1 at 100K also contains other interesting chemical elements:

Chlorine (Cl) 3 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Structure of Spin-Labelled T4 Lysozyme Mutant L118C-R1 at 100K (pdb code 5jdt). 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 Spin-Labelled T4 Lysozyme Mutant L118C-R1 at 100K, PDB code: 5jdt:

Potassium binding site 1 out of 1 in 5jdt

Go back to Potassium Binding Sites List in 5jdt
Potassium binding site 1 out of 1 in the Structure of Spin-Labelled T4 Lysozyme Mutant L118C-R1 at 100K


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of Spin-Labelled T4 Lysozyme Mutant L118C-R1 at 100K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K208

b:9.9
occ:0.56
HH A:TYR18 2.1 12.3 0.6
O A:HOH381 2.1 19.4 0.4
HH A:TYR18 2.6 9.1 0.4
OH A:TYR18 2.7 10.3 0.6
O A:HOH348 2.8 21.6 1.0
O A:HOH532 2.8 25.3 1.0
O A:HOH379 2.8 12.8 1.0
O A:GLU11 2.9 9.1 1.0
OE1 A:GLU11 3.1 9.8 1.0
HE2 A:TYR18 3.1 8.7 0.4
O A:HOH486 3.2 20.4 0.6
O A:HOH484 3.2 13.4 0.3
HA A:GLU11 3.2 9.1 1.0
OH A:TYR18 3.3 7.5 0.4
O A:HOH484 3.4 19.9 0.7
HE2 A:TYR18 3.7 12.1 0.6
C A:GLU11 3.7 7.9 1.0
O A:HOH305 3.8 8.5 0.6
CE2 A:TYR18 3.8 7.2 0.4
HB3 A:GLU11 3.8 9.5 1.0
HA2 A:GLY30 3.8 9.6 1.0
CA A:GLU11 3.9 7.6 1.0
CZ A:TYR18 3.9 9.7 0.6
CZ A:TYR18 4.0 7.2 0.4
CD A:GLU11 4.2 8.8 1.0
CE2 A:TYR18 4.2 10.1 0.6
O A:HOH305 4.2 9.7 0.4
HG21 A:THR26 4.3 8.8 1.0
CB A:GLU11 4.3 7.9 1.0
HB2 A:ASP20 4.4 10.0 1.0
H A:GLY30 4.4 8.8 1.0
HA3 A:GLY30 4.5 9.6 1.0
CA A:GLY30 4.5 8.0 1.0
HA A:ASP20 4.5 9.6 1.0
O A:HOH537 4.7 38.0 1.0
O A:HOH473 4.8 20.1 1.0
N A:GLY30 4.8 7.3 1.0
HG23 A:THR21 4.8 13.7 1.0
O A:ASP10 4.9 9.3 1.0
CG A:GLU11 4.9 8.3 1.0
HB3 A:ASP20 5.0 10.0 1.0
N A:GLY12 5.0 8.0 1.0

Reference:

P.Consentius, U.Gohlke, B.Loll, C.Alings, R.Muller, U.Heinemann, M.Kaupp, M.Wahl, T.Risse. Tracking Transient Conformational States of T4 Lysozyme at Room Temperature Combining X-Ray Crystallography and Site-Directed Spin Labeling. J.Am.Chem.Soc. V. 138 12868 2016.
ISSN: ESSN 1520-5126
PubMed: 27673570
DOI: 10.1021/JACS.6B05507
Page generated: Mon Aug 12 13:56:47 2024

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