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Magnesium in PDB 5lu5: A Quantum Half-Site Enzyme

Enzymatic activity of A Quantum Half-Site Enzyme

All present enzymatic activity of A Quantum Half-Site Enzyme:
5.3.1.28;

Protein crystallography data

The structure of A Quantum Half-Site Enzyme, PDB code: 5lu5 was solved by M.Vivoli, N.J.Harmer, J.Pang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 63.39 / 1.55
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 73.200, 83.810, 126.780, 90.00, 90.00, 90.00
R / Rfree (%) 16.1 / 18.7

Other elements in 5lu5:

The structure of A Quantum Half-Site Enzyme also contains other interesting chemical elements:

Sodium (Na) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the A Quantum Half-Site Enzyme (pdb code 5lu5). 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 A Quantum Half-Site Enzyme, PDB code: 5lu5:

Magnesium binding site 1 out of 1 in 5lu5

Go back to Magnesium Binding Sites List in 5lu5
Magnesium binding site 1 out of 1 in the A Quantum Half-Site Enzyme


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of A Quantum Half-Site Enzyme within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mg205

b:7.4
occ:1.00
O D:HOH448 2.0 51.2 1.0
O D:HOH301 2.4 26.3 1.0
O D:HOH475 2.6 11.0 1.0
O4 D:PG4202 2.7 30.1 0.7
O D:HOH417 2.9 34.0 1.0
O3 D:PG4202 3.0 30.1 0.7
O2 D:PG4202 3.0 28.3 0.7
C6 D:PG4202 3.5 27.6 0.7
C7 D:PG4202 3.5 28.0 0.7
C8 D:PG4202 3.5 30.2 0.7
C2 D:PG4202 3.7 24.6 0.7
C5 D:PG4202 3.7 31.6 0.7
O D:HOH411 3.8 35.1 1.0
C1 D:PG4202 3.9 28.3 0.7
C3 D:PG4202 3.9 33.7 0.7
C4 D:PG4202 4.0 32.1 0.7
O1 D:PG4202 4.6 32.0 0.7
OD1 D:ASP170 4.9 33.5 1.0
O5 D:PG4202 4.9 31.4 0.7
O D:HOH434 4.9 34.9 1.0

Reference:

M.Vivoli, J.Pang, N.J.Harmer. A Half-Site Multimeric Enzyme Achieves Its Cooperativity Without Conformational Changes. Sci Rep V. 7 16529 2017.
ISSN: ESSN 2045-2322
PubMed: 29184087
DOI: 10.1038/S41598-017-16421-2
Page generated: Tue Aug 12 14:44:36 2025

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