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Magnesium in PDB 6vz9: Structure of Proline Utilization A with the Fad Covalently Modified By L-Thiazolidine-2-Carboxylate

Enzymatic activity of Structure of Proline Utilization A with the Fad Covalently Modified By L-Thiazolidine-2-Carboxylate

All present enzymatic activity of Structure of Proline Utilization A with the Fad Covalently Modified By L-Thiazolidine-2-Carboxylate:
1.2.1.88; 1.5.5.2;

Protein crystallography data

The structure of Structure of Proline Utilization A with the Fad Covalently Modified By L-Thiazolidine-2-Carboxylate, PDB code: 6vz9 was solved by A.C.Campbell, J.J.Tanner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.44 / 1.52
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 100.961, 102.104, 126.379, 90.00, 106.35, 90.00
R / Rfree (%) 18 / 20.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of Proline Utilization A with the Fad Covalently Modified By L-Thiazolidine-2-Carboxylate (pdb code 6vz9). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Proline Utilization A with the Fad Covalently Modified By L-Thiazolidine-2-Carboxylate, PDB code: 6vz9:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 6vz9

Go back to Magnesium Binding Sites List in 6vz9
Magnesium binding site 1 out of 2 in the Structure of Proline Utilization A with the Fad Covalently Modified By L-Thiazolidine-2-Carboxylate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Proline Utilization A with the Fad Covalently Modified By L-Thiazolidine-2-Carboxylate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1303

b:29.7
occ:1.00
O A:HOH1488 2.0 28.5 1.0
O A:HOH1453 2.1 29.1 1.0
O2A A:NAD1302 2.1 29.2 1.0
O A:HOH1961 2.2 29.9 1.0
O A:HOH2323 2.2 32.2 1.0
O A:HOH2167 2.2 36.7 1.0
PA A:NAD1302 3.5 26.2 1.0
O A:HOH1945 3.6 28.8 1.0
O A:HOH2388 3.8 34.5 1.0
O1N A:NAD1302 3.9 26.6 1.0
O5B A:NAD1302 3.9 25.1 1.0
OE2 A:GLU733 4.3 32.1 1.0
OE1 A:GLU734 4.3 26.6 1.0
O A:HOH2390 4.3 32.5 1.0
O3 A:NAD1302 4.4 24.7 1.0
O1A A:NAD1302 4.5 25.8 1.0
PN A:NAD1302 4.6 26.3 1.0
O A:HOH1688 4.7 39.3 1.0
O2N A:NAD1302 4.8 24.8 1.0

Magnesium binding site 2 out of 2 in 6vz9

Go back to Magnesium Binding Sites List in 6vz9
Magnesium binding site 2 out of 2 in the Structure of Proline Utilization A with the Fad Covalently Modified By L-Thiazolidine-2-Carboxylate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Proline Utilization A with the Fad Covalently Modified By L-Thiazolidine-2-Carboxylate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1303

b:25.3
occ:1.00
O B:HOH1494 2.0 22.0 1.0
O B:HOH1819 2.0 23.1 1.0
O2A B:NAD1302 2.0 17.6 1.0
O B:HOH2393 2.1 27.9 1.0
O B:HOH2124 2.2 29.7 1.0
O B:HOH1846 2.2 31.5 1.0
PA B:NAD1302 3.4 16.4 1.0
O B:HOH1695 3.5 19.8 1.0
O1N B:NAD1302 3.8 16.9 1.0
O5B B:NAD1302 3.8 14.7 1.0
OE1 B:GLU733 4.3 21.9 1.0
O3 B:NAD1302 4.3 14.4 1.0
OE1 B:GLU734 4.3 20.3 1.0
O B:HOH2321 4.4 30.4 1.0
PN B:NAD1302 4.4 16.4 1.0
O1A B:NAD1302 4.5 13.7 1.0
O B:HOH2469 4.6 30.4 1.0
O2N B:NAD1302 4.6 15.1 1.0

Reference:

A.C.Campbell, D.F.Becker, K.S.Gates, J.J.Tanner. Covalent Modification of the Flavin in Proline Dehydrogenase By Thiazolidine-2-Carboxylate. Acs Chem.Biol. 2020.
ISSN: ESSN 1554-8937
PubMed: 32159324
DOI: 10.1021/ACSCHEMBIO.9B00935
Page generated: Tue Oct 1 22:17:38 2024

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