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Potassium in PDB 5lwo: Structure of Spin-Labelled T4 Lysozyme Mutant L115C-R119C-R1 at 100K

Enzymatic activity of Structure of Spin-Labelled T4 Lysozyme Mutant L115C-R119C-R1 at 100K

All present enzymatic activity of Structure of Spin-Labelled T4 Lysozyme Mutant L115C-R119C-R1 at 100K:
3.2.1.17;

Protein crystallography data

The structure of Structure of Spin-Labelled T4 Lysozyme Mutant L115C-R119C-R1 at 100K, PDB code: 5lwo 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) 18.30 / 1.18
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 60.170, 60.170, 97.720, 90.00, 90.00, 120.00
R / Rfree (%) 14.1 / 16.4

Other elements in 5lwo:

The structure of Structure of Spin-Labelled T4 Lysozyme Mutant L115C-R119C-R1 at 100K also contains other interesting chemical elements:

Chlorine (Cl) 4 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Structure of Spin-Labelled T4 Lysozyme Mutant L115C-R119C-R1 at 100K (pdb code 5lwo). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Structure of Spin-Labelled T4 Lysozyme Mutant L115C-R119C-R1 at 100K, PDB code: 5lwo:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 5lwo

Go back to Potassium Binding Sites List in 5lwo
Potassium binding site 1 out of 2 in the Structure of Spin-Labelled T4 Lysozyme Mutant L115C-R119C-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 L115C-R119C-R1 at 100K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K209

b:15.0
occ:0.63
HH A:TYR18 2.0 18.0 0.6
HH A:TYR18 2.5 10.4 0.4
OH A:TYR18 2.8 15.0 0.6
O A:HOH393 2.8 15.8 1.0
O A:GLU11 2.9 11.4 1.0
O A:HOH358 2.9 19.5 1.0
O A:HOH528 2.9 23.2 1.0
OE1 A:GLU11 3.0 12.6 1.0
HE2 A:TYR18 3.1 10.6 0.4
HA A:GLU11 3.2 11.5 1.0
O A:HOH481 3.3 20.5 1.0
O A:HOH486 3.3 25.0 1.0
OH A:TYR18 3.3 8.7 0.4
HE2 A:TYR18 3.5 17.4 0.6
HB3 A:GLU11 3.7 12.4 1.0
HA2 A:GLY30 3.7 11.7 1.0
C A:GLU11 3.7 10.0 1.0
CE2 A:TYR18 3.8 8.8 0.4
O A:HOH303 3.8 14.3 0.6
CZ A:TYR18 3.8 14.1 0.6
CA A:GLU11 3.9 9.6 1.0
CZ A:TYR18 4.0 8.9 0.4
CE2 A:TYR18 4.0 14.5 0.6
O A:HOH376 4.2 8.0 0.4
HG21 A:THR26 4.2 12.0 1.0
CD A:GLU11 4.2 11.1 1.0
CB A:GLU11 4.2 10.3 1.0
H A:GLY30 4.3 11.8 1.0
HA3 A:GLY30 4.3 11.7 1.0
CA A:GLY30 4.4 9.8 1.0
HB2 A:ASP20 4.4 13.2 1.0
HA A:ASP20 4.5 12.8 1.0
N A:GLY30 4.7 9.8 1.0
CG A:GLU11 4.8 10.6 1.0
HG23 A:THR21 4.9 16.0 1.0
O A:ASP10 4.9 11.9 1.0
O A:HOH466 4.9 19.5 1.0
HB3 A:ASP20 4.9 13.2 1.0
N A:GLY12 5.0 10.5 1.0

Potassium binding site 2 out of 2 in 5lwo

Go back to Potassium Binding Sites List in 5lwo
Potassium binding site 2 out of 2 in the Structure of Spin-Labelled T4 Lysozyme Mutant L115C-R119C-R1 at 100K


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Structure of Spin-Labelled T4 Lysozyme Mutant L115C-R119C-R1 at 100K within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K210

b:13.5
occ:0.34
O A:HOH335 2.2 11.2 0.7
O A:HOH347 2.4 20.6 1.0
O A:GLY30 2.7 10.2 1.0
O A:HOH506 2.9 22.0 0.6
HE1 A:PHE104 2.9 15.7 1.0
O A:PHE104 2.9 10.9 1.0
CE1 A:PHE104 3.0 13.1 1.0
O A:HOH478 3.1 22.8 1.0
CD1 A:PHE104 3.2 11.0 1.0
HD1 A:PHE104 3.2 13.2 1.0
O A:HOH397 3.5 17.2 1.0
CZ A:PHE104 3.7 13.2 1.0
H A:LEU32 3.9 11.2 1.0
C A:PHE104 3.9 9.7 1.0
C A:GLY30 3.9 9.5 1.0
CG A:PHE104 4.0 9.8 1.0
HZ A:PHE104 4.1 15.9 1.0
HA A:GLN105 4.1 12.1 1.0
HA3 A:GLY30 4.2 11.7 1.0
HA A:HIS31 4.3 10.9 1.0
O A:HOH523 4.4 16.2 0.4
HB2 A:LEU32 4.4 14.5 1.0
HA A:PHE104 4.5 11.4 1.0
CE2 A:PHE104 4.5 12.5 1.0
CD2 A:PHE104 4.6 10.8 1.0
OE2 A:GLU11 4.6 11.8 1.0
CA A:GLY30 4.6 9.8 1.0
N A:LEU32 4.7 9.3 1.0
CA A:PHE104 4.7 9.5 1.0
N A:GLN105 4.8 9.6 1.0
HB3 A:LEU32 4.8 14.5 1.0
CA A:GLN105 4.8 10.1 1.0
CB A:PHE104 4.9 9.3 1.0
O A:HOH337 4.9 12.6 1.0
N A:HIS31 4.9 9.2 1.0
HA2 A:GLY30 5.0 11.7 1.0

Reference:

P.Consentius, B.Loll, U.Gohlke, C.Alings, C.Muller, R.Muller, C.Teutloff, U.Heinemann, M.Kaupp, M.C.Wahl, T.Risse. Internal Dynamics of the 3-Pyrroline-N-Oxide Ring in Spin-Labeled Proteins. J Phys Chem Lett V. 8 1113 2017.
ISSN: ESSN 1948-7185
PubMed: 28221042
DOI: 10.1021/ACS.JPCLETT.6B02971
Page generated: Sat Aug 9 09:32:36 2025

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