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Magnesium in PDB 7x78: L-Fuculose 1-Phosphate Aldolase

Enzymatic activity of L-Fuculose 1-Phosphate Aldolase

All present enzymatic activity of L-Fuculose 1-Phosphate Aldolase:
4.1.2.17;

Protein crystallography data

The structure of L-Fuculose 1-Phosphate Aldolase, PDB code: 7x78 was solved by X.Lou, Q.Zhang, M.Bartlam, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.78 / 1.85
Space group P 4 21 2
Cell size a, b, c (Å), α, β, γ (°) 92.614, 92.614, 41.828, 90, 90, 90
R / Rfree (%) 16.4 / 21.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the L-Fuculose 1-Phosphate Aldolase (pdb code 7x78). 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 L-Fuculose 1-Phosphate Aldolase, PDB code: 7x78:

Magnesium binding site 1 out of 1 in 7x78

Go back to Magnesium Binding Sites List in 7x78
Magnesium binding site 1 out of 1 in the L-Fuculose 1-Phosphate Aldolase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of L-Fuculose 1-Phosphate Aldolase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg304

b:9.9
occ:1.00
NE2 A:HIS94 2.1 19.8 1.0
OE2 A:GLU73 2.2 32.5 1.0
NE2 A:HIS92 2.2 17.2 1.0
NE2 A:HIS155 2.2 22.3 1.0
O A:HOH401 2.5 41.4 1.0
CD A:GLU73 2.9 38.1 1.0
OE1 A:GLU73 2.9 40.0 1.0
CE1 A:HIS94 3.0 24.9 1.0
CD2 A:HIS155 3.1 23.1 1.0
CE1 A:HIS92 3.1 16.0 1.0
CD2 A:HIS94 3.2 21.8 1.0
CD2 A:HIS92 3.2 21.7 1.0
CE1 A:HIS155 3.3 24.4 1.0
ND1 A:HIS94 4.2 21.5 1.0
ND1 A:HIS92 4.3 15.8 1.0
CG A:HIS155 4.3 20.6 1.0
CG A:HIS94 4.3 19.1 1.0
CG A:HIS92 4.3 19.4 1.0
ND1 A:HIS155 4.3 22.7 1.0
CG A:GLU73 4.4 32.5 1.0
O A:ALA27 4.4 53.3 1.0
CZ A:PHE76 4.9 19.4 1.0
ND2 A:ASN29 5.0 25.5 1.0

Reference:

X.Lou, J.Zhang, S.Liu, R.Wang, W.Li, R.Liu, Q.Zhang, M.Bartlam. Structural Characterization of An L-Fuculose-1-Phosphate Aldolase From Klebsiella Pneumoniae. Biochem.Biophys.Res.Commun. V. 607 15 2022.
ISSN: ESSN 1090-2104
PubMed: 35366538
DOI: 10.1016/J.BBRC.2022.03.127
Page generated: Thu Oct 3 11:51:49 2024

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