Magnesium in PDB 8t7v: 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: 8t7v 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) 46.24 / 2.25
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 57.546, 77.805, 58.827, 90, 92.19, 90
R / Rfree (%) 20.2 / 25

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 8t7v). 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: 8t7v:

Magnesium binding site 1 out of 1 in 8t7v

Go back to Magnesium Binding Sites List in 8t7v
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:39.8
occ:1.00
 O1G B:GNP201 2.1 44.1 1.0
O1B B:GNP201 2.1 32.7 1.0
OG B:SER17 2.1 30.5 1.0
O B:HOH302 2.1 34.7 1.0
O B:HOH301 2.2 29.8 1.0
OG1 B:THR35 2.3 39.2 1.0
CB B:THR35 3.1 35.8 1.0
PG B:GNP201 3.3 34.6 1.0
CB B:SER17 3.3 26.8 1.0
PB B:GNP201 3.3 36.0 1.0
N3B B:GNP201 3.5 25.3 1.0
OD2 B:ASP57 3.8 56.1 1.0
N B:THR35 3.8 38.7 1.0
N B:SER17 3.9 29.2 1.0
O2G B:GNP201 4.0 36.1 1.0
O2A B:GNP201 4.0 32.4 1.0
CA B:THR35 4.0 37.8 1.0
CG2 B:THR35 4.2 44.8 1.0
CA B:SER17 4.2 31.6 1.0
OD1 B:ASP57 4.2 52.9 1.0
O2B B:GNP201 4.2 34.8 1.0
O B:ASP33 4.3 53.8 1.0
CG B:ASP57 4.4 43.1 1.0
NH2 A:ARG452 4.4 66.4 1.0
O3A B:GNP201 4.4 40.5 1.0
O3G B:GNP201 4.5 35.2 1.0
O B:THR58 4.5 33.8 1.0
PA B:GNP201 4.6 30.8 1.0
O1A B:GNP201 4.7 31.3 1.0
C B:PRO34 4.8 48.9 1.0
CB B:LYS16 4.9 30.3 1.0
C B:LYS16 5.0 35.1 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 20:31:40 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy