Magnesium in PDB 8aau: Lim Domain Kinase 1 (LIMK1) Bound to LIMKI3

Enzymatic activity of Lim Domain Kinase 1 (LIMK1) Bound to LIMKI3

All present enzymatic activity of Lim Domain Kinase 1 (LIMK1) Bound to LIMKI3:
2.7.11.1;

Protein crystallography data

The structure of Lim Domain Kinase 1 (LIMK1) Bound to LIMKI3, PDB code: 8aau was solved by S.Mathea, E.Salah, T.Hanke, S.Knapp, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 68.71 / 1.74
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 85.668, 85.668, 182.108, 90, 90, 120
R / Rfree (%) 21.1 / 24

Other elements in 8aau:

The structure of Lim Domain Kinase 1 (LIMK1) Bound to LIMKI3 also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms
Fluorine (F) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Lim Domain Kinase 1 (LIMK1) Bound to LIMKI3 (pdb code 8aau). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Lim Domain Kinase 1 (LIMK1) Bound to LIMKI3, PDB code: 8aau:

Magnesium binding site 1 out of 1 in 8aau

Go back to Magnesium Binding Sites List in 8aau
Magnesium binding site 1 out of 1 in the Lim Domain Kinase 1 (LIMK1) Bound to LIMKI3


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Lim Domain Kinase 1 (LIMK1) Bound to LIMKI3 within 5.0Å range:
probe atom residue distance (Å) B Occ
L:Mg706

b:42.4
occ:1.00
O L:HOH875 2.1 41.8 1.0
O L:HOH869 2.1 45.0 1.0
O L:HOH822 2.2 40.9 1.0
OD2 L:ASP478 2.2 41.5 1.0
OD2 L:ASP460 2.2 39.6 1.0
O L:HOH883 2.2 41.5 1.0
CG L:ASP478 3.2 39.4 1.0
CG L:ASP460 3.4 37.8 1.0
OD1 L:ASP478 3.5 36.0 1.0
O L:HOH811 4.0 41.4 1.0
OD1 L:ASP460 4.2 35.6 1.0
ND2 L:ASN465 4.2 32.1 1.0
CB L:ASP460 4.5 31.5 1.0
CB L:ASP478 4.5 35.2 1.0
CD1 L:LEU481 4.7 38.1 1.0

Reference:

S.Mathea, E.Salah, T.Hanke, S.Knapp. Lim Domain Kinase 1 (LIMK1) Bound to LIMKI3 To Be Published.
Page generated: Fri Apr 7 06:05:18 2023

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