Magnesium in PDB 3pff: Truncated Human Atp-Citrate Lyase with Adp and Tartrate Bound

All present enzymatic activity of Truncated Human Atp-Citrate Lyase with Adp and Tartrate Bound:
2.3.3.8;

The structure of Truncated Human Atp-Citrate Lyase with Adp and Tartrate Bound, PDB code: 3pff was solved by M.E.Fraser, T.Sun, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.97 / 2.30
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	167.540, 61.700, 107.980, 90.00, 125.47, 90.00
R / Rfree (%)	16.8 / 22.8

The binding sites of Magnesium atom in the Truncated Human Atp-Citrate Lyase with Adp and Tartrate Bound (pdb code 3pff). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Truncated Human Atp-Citrate Lyase with Adp and Tartrate Bound, PDB code: 3pff:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Truncated Human Atp-Citrate Lyase with Adp and Tartrate Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Truncated Human Atp-Citrate Lyase with Adp and Tartrate Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg830 b:51.4 occ:1.00 O A:ALA262 2.7 43.2 1.0 O A:SER260 2.7 46.4 1.0 O A:HOH1104 2.7 49.9 1.0 OD1 A:ASP257 2.8 32.6 1.0 O A:ASP257 2.8 33.9 1.0 C A:ALA262 3.5 37.8 1.0 CG A:ASP257 3.7 32.0 1.0 O A:GLY261 3.8 47.0 1.0 C A:SER260 3.8 47.3 1.0 C A:ASP257 3.9 36.5 1.0 C A:GLY261 3.9 44.6 1.0 CA A:SER263 4.0 30.9 1.0 N A:SER263 4.1 30.8 1.0 OD2 A:ASP257 4.2 33.9 1.0 N A:ALA262 4.4 41.5 1.0 CA A:GLY261 4.4 42.5 1.0 CA A:ASP257 4.4 28.4 1.0 OG A:SER260 4.5 48.9 1.0 N A:GLY261 4.5 50.3 1.0 CA A:ALA262 4.6 36.2 1.0 CB A:ASP257 4.6 30.2 1.0 N A:LEU264 4.8 32.9 1.0 CA A:SER260 4.9 44.6 1.0 CB A:SER263 4.9 29.4 1.0 N A:SER260 4.9 47.8 1.0 N A:ALA258 4.9 38.5 1.0 C A:SER263 5.0 33.7 1.0

Magnesium binding site 2 out of 2 in the Truncated Human Atp-Citrate Lyase with Adp and Tartrate Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Truncated Human Atp-Citrate Lyase with Adp and Tartrate Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg831 b:26.9 occ:1.00 O1A A:ADP833 2.1 25.7 1.0 O A:ASN203 2.1 19.8 1.0 O2B A:ADP833 2.2 23.4 1.0 OD2 A:ASP216 2.3 23.5 1.0 O A:HOH1168 2.3 22.8 1.0 O A:HOH1144 2.4 26.5 1.0 CG A:ASP216 3.2 28.9 1.0 PA A:ADP833 3.2 28.2 1.0 C A:ASN203 3.3 19.9 1.0 PB A:ADP833 3.4 24.4 1.0 CB A:ASP216 3.5 22.7 1.0 O3A A:ADP833 3.6 27.2 1.0 O A:HOH1155 3.6 33.0 1.0 O A:HOH1135 3.9 36.5 1.0 CD A:PRO204 3.9 19.7 1.0 N A:PRO204 4.1 20.1 1.0 O2A A:ADP833 4.2 25.4 1.0 O A:HOH1154 4.2 26.4 1.0 O A:HOH1189 4.3 34.0 1.0 O1B A:ADP833 4.3 28.3 1.0 ND2 A:ASN203 4.3 15.3 1.0 OD1 A:ASP216 4.4 30.4 1.0 CB A:ASN203 4.4 22.4 1.0 CA A:ASN203 4.4 20.9 1.0 O3B A:ADP833 4.4 24.0 1.0 O5' A:ADP833 4.5 27.1 1.0 CG A:ASN203 4.5 24.1 1.0 C5' A:ADP833 4.7 24.5 1.0 N A:ASN203 4.9 17.1 1.0 O3' A:ADP833 4.9 25.6 1.0 NH2 A:ARG66 5.0 22.2 1.0 CA A:ASP216 5.0 22.5 1.0

T.Sun, K.Hayakawa, M.E.Fraser. Adp-MG2+ Bound to the Atp-Grasp Domain of Atp-Citrate Lyase. Acta Crystallogr.,Sect.F V. 67 1168 2011.
ISSN: ESSN 1744-3091
PubMed: 22102020
DOI: 10.1107/S1744309111028363