Magnesium in PDB 4e1b: Re-Refinement of Pdb Entry 2EQA - SUA5 Protein From Sulfolobus Tokodaii with Bound Threonylcarbamoyladenylate

The structure of Re-Refinement of Pdb Entry 2EQA - SUA5 Protein From Sulfolobus Tokodaii with Bound Threonylcarbamoyladenylate, PDB code: 4e1b was solved by C.Parthier, S.Goerlich, F.Jaenecke, C.Breithaupt, U.Braeuer, U.Fandrich, D.Clausnitzer, U.F.Wehmeier, C.Boettcher, D.Scheel, M.T.Stubbs, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.87 / 1.80
Space group	C 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	85.391, 120.843, 67.552, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 21.7

The binding sites of Magnesium atom in the Re-Refinement of Pdb Entry 2EQA - SUA5 Protein From Sulfolobus Tokodaii with Bound Threonylcarbamoyladenylate (pdb code 4e1b). 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 Re-Refinement of Pdb Entry 2EQA - SUA5 Protein From Sulfolobus Tokodaii with Bound Threonylcarbamoyladenylate, PDB code: 4e1b:

Magnesium binding site 1 out of 1 in the Re-Refinement of Pdb Entry 2EQA - SUA5 Protein From Sulfolobus Tokodaii with Bound Threonylcarbamoyladenylate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Re-Refinement of Pdb Entry 2EQA - SUA5 Protein From Sulfolobus Tokodaii with Bound Threonylcarbamoyladenylate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg2001 b:20.1 occ:1.00 OG A:SER144 2.2 10.4 1.0 OP3 A:TXA2002 2.3 17.8 1.0 O A:HOH2132 2.4 19.8 1.0 O A:HOH2123 2.5 18.0 1.0 O A:HOH2107 2.5 19.1 1.0 O A:HOH2253 2.6 30.9 1.0 CB A:SER144 3.4 10.7 1.0 P A:TXA2002 3.6 19.9 1.0 OP1 A:TXA2002 3.8 19.3 1.0 OD1 A:ASN146 4.1 21.4 1.0 NH1 A:ARG59 4.1 8.7 1.0 O A:HOH2241 4.1 28.2 1.0 N A:SER144 4.1 8.4 1.0 OG A:SER152 4.2 12.7 1.0 CA A:SER144 4.3 9.6 1.0 OCA A:TXA2002 4.4 19.1 1.0 NZ A:LYS57 4.5 10.7 1.0 O5' A:TXA2002 4.6 21.0 1.0 ND2 A:ASN146 4.7 22.9 1.0 OP2 A:TXA2002 4.7 20.0 1.0 OE2 A:GLU181 4.8 12.7 1.0 CCA A:TXA2002 4.8 20.0 1.0 CG A:ASN146 4.8 16.9 1.0 O A:SER144 4.9 10.5 1.0 C A:SER144 5.0 10.6 1.0

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