Magnesium in PDB 5tdz: Tev Cleaved Human Atp Citrate Lyase Bound to Tartrate and Adp

All present enzymatic activity of Tev Cleaved Human Atp Citrate Lyase Bound to Tartrate and Adp:
2.3.3.8;

The structure of Tev Cleaved Human Atp Citrate Lyase Bound to Tartrate and Adp, PDB code: 5tdz was solved by J.Hu, M.E.Fraser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.38 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.672, 84.291, 195.594, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 22.2

The binding sites of Magnesium atom in the Tev Cleaved Human Atp Citrate Lyase Bound to Tartrate and Adp (pdb code 5tdz). 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 Tev Cleaved Human Atp Citrate Lyase Bound to Tartrate and Adp, PDB code: 5tdz:

Magnesium binding site 1 out of 1 in the Tev Cleaved Human Atp Citrate Lyase Bound to Tartrate and Adp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Tev Cleaved Human Atp Citrate Lyase Bound to Tartrate and Adp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg903 b:42.4 occ:1.00 HOA2 A:ADP902 1.7 41.4 1.0 O1B A:ADP902 1.9 46.2 1.0 OD2 A:ASP216 2.1 37.0 1.0 O A:HOH1078 2.1 41.1 1.0 O A:ASN203 2.2 21.3 1.0 O2A A:ADP902 2.3 34.5 1.0 O A:HOH1121 2.3 39.0 1.0 CG A:ASP216 3.2 35.5 1.0 PB A:ADP902 3.2 40.7 1.0 HB3 A:ASN203 3.2 27.8 1.0 C A:ASN203 3.4 23.8 1.0 PA A:ADP902 3.4 39.8 1.0 HB3 A:ASP216 3.5 29.5 1.0 O3A A:ADP902 3.5 45.7 1.0 HB2 A:ASP216 3.7 29.5 1.0 CB A:ASP216 3.7 24.6 1.0 HD3 A:PRO204 3.7 34.3 1.0 HD22 A:ASN203 3.9 42.9 1.0 CB A:ASN203 3.9 23.2 1.0 ND2 A:ASN203 4.0 35.8 1.0 O A:HOH1012 4.0 49.7 1.0 CG A:ASN203 4.0 25.3 1.0 O1A A:ADP902 4.1 37.6 1.0 O A:HOH1054 4.1 39.3 1.0 H5'2 A:ADP902 4.2 49.3 1.0 O2B A:ADP902 4.2 31.2 1.0 O3B A:ADP902 4.2 38.6 1.0 OD1 A:ASP216 4.2 40.0 1.0 CA A:ASN203 4.2 25.1 1.0 HH12 A:ARG65 4.3 74.5 1.0 O A:HOH1225 4.3 38.4 1.0 N A:PRO204 4.3 16.9 1.0 CD A:PRO204 4.3 28.6 1.0 O A:HOH1181 4.3 36.0 1.0 HH21 A:ARG66 4.4 31.2 1.0 HD2 A:PRO204 4.4 34.3 1.0 HOB2 A:ADP902 4.4 37.5 1.0 HD21 A:ASN203 4.4 42.9 1.0 HH11 A:ARG65 4.4 74.5 1.0 H A:ASN203 4.5 24.7 1.0 O3' A:ADP902 4.5 44.4 1.0 H3' A:ADP902 4.5 53.6 1.0 O5' A:ADP902 4.6 45.6 1.0 NH1 A:ARG65 4.6 62.0 1.0 OD1 A:ASN203 4.7 25.2 1.0 HOB3 A:ADP902 4.7 46.3 1.0 HB2 A:ASN203 4.8 27.8 1.0 N A:ASN203 4.9 20.6 1.0 C5' A:ADP902 5.0 41.1 1.0

J.Hu, A.Komakula, M.E.Fraser. Binding of Hydroxycitrate to Human Atp-Citrate Lyase. Acta Crystallogr D Struct V. 73 660 2017BIOL.
ISSN: ISSN 2059-7983
PubMed: 28777081
DOI: 10.1107/S2059798317009871