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Magnesium in PDB 1qf5: Design, Synthesis, and X-Ray Crystal Structure of An Enzyme Bound Bisubstrate Hybrid Inhibitor of Adenylosuccinate Synthetase

Enzymatic activity of Design, Synthesis, and X-Ray Crystal Structure of An Enzyme Bound Bisubstrate Hybrid Inhibitor of Adenylosuccinate Synthetase

All present enzymatic activity of Design, Synthesis, and X-Ray Crystal Structure of An Enzyme Bound Bisubstrate Hybrid Inhibitor of Adenylosuccinate Synthetase:
6.3.4.4;

Protein crystallography data

The structure of Design, Synthesis, and X-Ray Crystal Structure of An Enzyme Bound Bisubstrate Hybrid Inhibitor of Adenylosuccinate Synthetase, PDB code: 1qf5 was solved by S.Hanessian, P.-P.Lu, J.-Y.Sanceau, P.Chemla, L.Prade, K.Gohda, S.W.Cowan-Jacob, R.Fonne-Pfister, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 2.00
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 81.750, 81.750, 158.700, 90.00, 90.00, 120.00
R / Rfree (%) 19.6 / 22.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Design, Synthesis, and X-Ray Crystal Structure of An Enzyme Bound Bisubstrate Hybrid Inhibitor of Adenylosuccinate Synthetase (pdb code 1qf5). 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 Design, Synthesis, and X-Ray Crystal Structure of An Enzyme Bound Bisubstrate Hybrid Inhibitor of Adenylosuccinate Synthetase, PDB code: 1qf5:

Magnesium binding site 1 out of 1 in 1qf5

Go back to Magnesium Binding Sites List in 1qf5
Magnesium binding site 1 out of 1 in the Design, Synthesis, and X-Ray Crystal Structure of An Enzyme Bound Bisubstrate Hybrid Inhibitor of Adenylosuccinate Synthetase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Design, Synthesis, and X-Ray Crystal Structure of An Enzyme Bound Bisubstrate Hybrid Inhibitor of Adenylosuccinate Synthetase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg433

b:34.8
occ:1.00
 OD1 A:ASP13 1.9 43.0 1.0
O A:GLY40 2.0 39.2 1.0
O4 A:PO4432 2.2 35.0 1.0
O2A A:GDP434 2.2 54.0 1.0
OBA A:RPL435 2.3 52.9 1.0
O2B A:GDP434 2.5 39.5 1.0
CBA A:RPL435 2.8 50.2 1.0
C A:GLY40 3.1 35.3 1.0
CG A:ASP13 3.1 40.4 1.0
O1 A:PO4432 3.2 40.3 1.0
P A:PO4432 3.2 38.9 1.0
PA A:GDP434 3.6 49.4 1.0
N A:GLY40 3.6 33.7 1.0
CA A:GLY40 3.7 35.4 1.0
PB A:GDP434 3.8 38.2 1.0
OD2 A:ASP13 3.9 39.0 1.0
CB A:ASP13 4.0 37.1 1.0
O3 A:PO4432 4.0 37.9 1.0
O2 A:PO4432 4.0 34.4 1.0
O3A A:GDP434 4.0 44.1 1.0
CA A:ASP13 4.0 34.2 1.0
NAA A:RPL435 4.1 51.5 1.0
N A:HIS41 4.2 35.4 1.0
CD2 A:HIS41 4.2 29.2 1.0
OAA A:RPL435 4.3 45.4 1.0
N A:ASP13 4.3 35.3 1.0
O3B A:GDP434 4.4 40.5 1.0
CB A:ALA299 4.4 40.6 1.0
O1A A:GDP434 4.5 56.3 1.0
CA A:HIS41 4.6 35.8 1.0
O5' A:GDP434 4.6 52.4 1.0
NH1 A:ARG305 4.7 40.6 1.0
C6A A:RPL435 4.8 41.2 1.0
C A:ALA39 4.8 32.6 1.0
O1B A:GDP434 5.0 44.0 1.0

Reference:

S.Hanessian, P.P.Lu, J.Y.Sanceau, P.Chemla, K.Gohda, R.Fonne-Pfister, L.Prade, S.W.Cowan-Jacob. An Enzyme-Bound Bisubstrate Hybrid Inhibitor of Adenylosuccinate Synthetase Angew.Chem.Int.Ed.Engl. V. 38 3159 1999.
ISSN: ISSN 1433-7851
PubMed: 10556888
DOI: 10.1002/(SICI)1521-3773(19991102)38:21<3159::AID-ANIE3159>3.0.CO;2-2
Page generated: Tue Aug 13 11:49:34 2024

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