Magnesium in PDB 3vez: Crystal Structure of the O-Carbamoyltransferase Tobz K443A Variant in Complex with Atp, Adp and Carbamoyl Phosphate

The structure of Crystal Structure of the O-Carbamoyltransferase Tobz K443A Variant in Complex with Atp, Adp and Carbamoyl Phosphate, PDB code: 3vez was solved by C.Parthier, M.T.Stubbs, S.Goerlich, F.Jaenecke, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.36 / 2.40
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	99.147, 99.147, 281.156, 90.00, 90.00, 120.00
R / Rfree (%)	18.4 / 23.9

The structure of Crystal Structure of the O-Carbamoyltransferase Tobz K443A Variant in Complex with Atp, Adp and Carbamoyl Phosphate also contains other interesting chemical elements:

Potassium	(K)	1 atom
Iron	(Fe)	1 atom

The binding sites of Magnesium atom in the Crystal Structure of the O-Carbamoyltransferase Tobz K443A Variant in Complex with Atp, Adp and Carbamoyl Phosphate (pdb code 3vez). 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 Crystal Structure of the O-Carbamoyltransferase Tobz K443A Variant in Complex with Atp, Adp and Carbamoyl Phosphate, PDB code: 3vez:

Magnesium binding site 1 out of 1 in the Crystal Structure of the O-Carbamoyltransferase Tobz K443A Variant in Complex with Atp, Adp and Carbamoyl Phosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the O-Carbamoyltransferase Tobz K443A Variant in Complex with Atp, Adp and Carbamoyl Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg602 b:43.6 occ:1.00 OG A:SER530 2.4 24.1 1.0 O1B A:ATP604 2.5 36.6 0.7 O2P A:CP605 2.7 24.1 1.0 O A:HOH965 2.8 32.6 1.0 O A:HOH851 2.8 27.8 1.0 O A:HOH966 3.0 28.6 1.0 O3G A:ATP604 3.1 43.4 0.7 O3B A:ATP604 3.2 55.2 0.7 PB A:ATP604 3.3 58.9 0.7 O2G A:ATP604 3.4 44.6 0.7 PG A:ATP604 3.5 46.5 0.7 CB A:SER530 3.7 25.8 1.0 OD1 A:ASN532 3.8 27.8 1.0 ND2 A:ASN532 3.9 25.5 1.0 P A:CP605 4.1 22.1 1.0 NH1 A:ARG445 4.2 51.9 1.0 O2B A:ATP604 4.2 43.8 0.7 CG A:ASN532 4.3 29.2 1.0 N A:SER530 4.4 24.9 1.0 CA A:SER530 4.5 26.4 1.0 O A:SER530 4.5 24.8 1.0 O3A A:ATP604 4.6 45.4 0.7 OG1 A:THR529 4.7 26.2 1.0 O1P A:CP605 4.7 27.4 1.0 O3P A:CP605 4.7 25.0 1.0 C A:SER530 4.9 26.3 1.0 NH2 A:ARG449 4.9 36.0 1.0 O1G A:ATP604 5.0 46.7 0.7

C.Parthier, S.Gorlich, F.Jaenecke, C.Breithaupt, U.Brauer, U.Fandrich, D.Clausnitzer, U.F.Wehmeier, C.Bottcher, D.Scheel, M.T.Stubbs. The O-Carbamoyltransferase Tobz Catalyzes An Ancient Enzymatic Reaction. Angew.Chem.Int.Ed.Engl. V. 51 4046 2012.
ISSN: ISSN 1433-7851
PubMed: 22383337
DOI: 10.1002/ANIE.201108896