Magnesium in PDB 1obd: Saicar-Synthase Complexed with Atp

All present enzymatic activity of Saicar-Synthase Complexed with Atp:
6.3.2.6;

The structure of Saicar-Synthase Complexed with Atp, PDB code: 1obd was solved by S.V.Antonyuk, A.I.Grebenko, V.M.Levdikov, D.V.Urusova, W.R.Melik-Adamyan, V.S.Lamzin, K.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	61.480, 63.050, 79.820, 90.00, 90.00, 90.00
R / Rfree (%)	15.2 / 19.5

The binding sites of Magnesium atom in the Saicar-Synthase Complexed with Atp (pdb code 1obd). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Saicar-Synthase Complexed with Atp, PDB code: 1obd:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Saicar-Synthase Complexed with Atp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Saicar-Synthase Complexed with Atp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg310 b:24.3 occ:1.00 O A:HOH2397 1.9 24.4 1.0 O2G A:ATP307 2.0 26.6 1.0 O2A A:ATP307 2.0 24.5 1.0 O2B A:ATP307 2.2 26.6 1.0 PB A:ATP307 3.2 24.3 1.0 PA A:ATP307 3.3 23.1 1.0 PG A:ATP307 3.3 24.9 1.0 O3A A:ATP307 3.5 24.9 1.0 O3B A:ATP307 3.6 25.0 1.0 OD1 A:ASP233 3.9 18.4 1.0 O A:HOH2516 4.0 37.9 1.0 OD2 A:ASP233 4.0 25.0 1.0 O A:HOH2513 4.2 34.3 1.0 O3G A:ATP307 4.2 26.5 1.0 O5' A:ATP307 4.2 25.4 1.0 O1A A:ATP307 4.3 24.4 1.0 OE1 A:GLU219 4.3 26.2 1.0 O1G A:ATP307 4.4 24.2 1.0 C5' A:ATP307 4.4 24.5 1.0 C3' A:ATP307 4.4 23.6 1.0 CG A:ASP233 4.4 20.5 1.0 O A:HOH2182 4.5 42.9 1.0 NZ A:LYS217 4.5 31.4 1.0 O1B A:ATP307 4.5 27.1 1.0 NH2 A:ARG21 4.6 25.1 1.0 O A:HOH2380 4.8 37.4 1.0 C2' A:ATP307 4.8 23.2 1.0 O A:HOH2381 5.0 46.6 1.0

Magnesium binding site 2 out of 2 in the Saicar-Synthase Complexed with Atp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Saicar-Synthase Complexed with Atp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg311 b:35.7 occ:1.00 OG A:SER61 2.1 23.5 0.8 OE2 A:GLU234 2.2 38.0 1.0 OG A:SER61 2.4 15.1 0.2 O A:HOH2150 2.7 27.0 1.0 CA A:GLU234 2.7 21.6 1.0 N A:VAL235 2.8 16.4 1.0 CD A:GLU234 2.9 32.3 1.0 CB A:SER61 3.1 16.1 0.8 CB A:SER61 3.2 15.4 0.2 C A:GLU234 3.2 18.1 1.0 CB A:GLU234 3.2 22.8 1.0 CG A:GLU234 3.3 29.4 1.0 CG2 A:THR237 3.7 15.7 1.0 OE1 A:GLU234 3.9 26.8 1.0 O A:HOH2399 3.9 26.9 1.0 N A:GLU234 4.0 21.0 1.0 O A:ASP233 4.0 24.9 1.0 CA A:VAL235 4.0 15.2 1.0 O A:HOH2067 4.2 23.8 1.0 O A:VAL235 4.2 13.1 1.0 NH1 A:ARG21 4.2 25.0 1.0 O A:GLU234 4.4 18.3 1.0 O A:HOH2398 4.4 22.3 1.0 CA A:SER61 4.4 15.5 1.0 C A:VAL235 4.4 13.9 1.0 C A:ASP233 4.5 20.8 1.0 CB A:VAL235 4.7 16.8 1.0 O A:LEU57 4.8 13.7 1.0 CG2 A:VAL235 5.0 18.7 1.0

S.V.Antonyuk, A.I.Grebenko, V.M.Levdikov, D.V.Urusova, W.R.Melik-Adamyan, V.S.Lamzin, K.Wilson. X-Ray Structure of Saicar-Synthase Complexed with Atp Kristallografiya V. 46 620 2001.
ISSN: ISSN 0023-4761