Magnesium in PDB 8su8: Co-Crystal Structure of KRIT1 with A 1-Hydroxy 2-Naphthaldehyde Derivative (6-(Furan-2-Yl)-2-Hydroxy-1-Naphthaldehyde).

Enzymatic activity of Co-Crystal Structure of KRIT1 with A 1-Hydroxy 2-Naphthaldehyde Derivative (6-(Furan-2-Yl)-2-Hydroxy-1-Naphthaldehyde).

All present enzymatic activity of Co-Crystal Structure of KRIT1 with A 1-Hydroxy 2-Naphthaldehyde Derivative (6-(Furan-2-Yl)-2-Hydroxy-1-Naphthaldehyde).:
3.6.5.2;

Protein crystallography data

The structure of Co-Crystal Structure of KRIT1 with A 1-Hydroxy 2-Naphthaldehyde Derivative (6-(Furan-2-Yl)-2-Hydroxy-1-Naphthaldehyde)., PDB code: 8su8 was solved by J.G.H.Bruystens, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.65 / 2.01
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 57.5, 77.536, 58.431, 90, 91.6, 90
R / Rfree (%) 20.4 / 23.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Co-Crystal Structure of KRIT1 with A 1-Hydroxy 2-Naphthaldehyde Derivative (6-(Furan-2-Yl)-2-Hydroxy-1-Naphthaldehyde). (pdb code 8su8). 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 Co-Crystal Structure of KRIT1 with A 1-Hydroxy 2-Naphthaldehyde Derivative (6-(Furan-2-Yl)-2-Hydroxy-1-Naphthaldehyde)., PDB code: 8su8:

Magnesium binding site 1 out of 1 in 8su8

Go back to Magnesium Binding Sites List in 8su8
Magnesium binding site 1 out of 1 in the Co-Crystal Structure of KRIT1 with A 1-Hydroxy 2-Naphthaldehyde Derivative (6-(Furan-2-Yl)-2-Hydroxy-1-Naphthaldehyde).


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Co-Crystal Structure of KRIT1 with A 1-Hydroxy 2-Naphthaldehyde Derivative (6-(Furan-2-Yl)-2-Hydroxy-1-Naphthaldehyde). within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg200

b:38.6
occ:1.00
 O1B B:GNP201 2.0 28.8 1.0
OG B:SER17 2.0 35.2 1.0
OG1 B:THR35 2.0 42.9 1.0
O1G B:GNP201 2.1 38.7 1.0
O B:HOH306 2.1 38.2 1.0
O B:HOH304 2.2 30.1 1.0
CB B:SER17 3.1 31.2 1.0
CB B:THR35 3.2 32.1 1.0
PB B:GNP201 3.2 36.6 1.0
PG B:GNP201 3.3 38.4 1.0
N3B B:GNP201 3.4 34.9 1.0
N B:SER17 3.8 28.9 1.0
OD2 B:ASP57 3.9 43.0 1.0
N B:THR35 4.0 36.5 1.0
O2G B:GNP201 4.0 34.7 1.0
CA B:SER17 4.0 34.6 1.0
O2B B:GNP201 4.1 37.5 1.0
O2A B:GNP201 4.1 29.1 1.0
CG2 B:THR35 4.2 41.7 1.0
CA B:THR35 4.2 39.0 1.0
O A:HOH905 4.2 51.0 1.0
OD1 B:ASP57 4.3 36.4 1.0
O3A B:GNP201 4.4 32.6 1.0
O3G B:GNP201 4.5 42.4 1.0
O B:THR58 4.5 30.9 1.0
CG B:ASP57 4.5 37.4 1.0
O B:ASP33 4.5 47.3 1.0
PA B:GNP201 4.5 40.6 1.0
O1A B:GNP201 4.6 34.2 1.0
NH2 A:ARG452 4.6 83.9 1.0
CB B:LYS16 4.8 28.6 1.0
C B:LYS16 4.9 33.2 1.0

Reference:

K.R.Francisco, J.Bruystens, C.Varricchio, S.Mccurdy, J.Wu, M.A.Lopez-Ramirez, M.Ginsberg, C.R.Caffrey, A.Brancale, A.R.Gingras, M.S.Hixon, C.Ballatore. Targeted Reversible Covalent Modification of A Noncatalytic Lysine of the Krev Interaction Trapped 1 Protein Enables Site-Directed Screening For Protein-Protein Interaction Inhibitors. Acs Pharmacol Transl Sci V. 6 1651 2023.
ISSN: ESSN 2575-910
PubMed: 37974623
DOI: 10.1021/ACSPTSCI.3C00156
Page generated: Fri Oct 4 20:14:29 2024

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