Magnesium in PDB 2fmt: Methionyl-Trnafmet Formyltransferase Complexed with Formyl- Methionyl-Trnafmet

All present enzymatic activity of Methionyl-Trnafmet Formyltransferase Complexed with Formyl- Methionyl-Trnafmet:
2.1.2.9;

The structure of Methionyl-Trnafmet Formyltransferase Complexed with Formyl- Methionyl-Trnafmet, PDB code: 2fmt was solved by E.Schmitt, Y.Mechulam, S.Blanquet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.00 / 2.80
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	201.710, 68.060, 86.350, 90.00, 90.00, 90.00
R / Rfree (%)	24.7 / 29.2

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

Magnesium binding site 1 out of 2 in the Methionyl-Trnafmet Formyltransferase Complexed with Formyl- Methionyl-Trnafmet


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Methionyl-Trnafmet Formyltransferase Complexed with Formyl- Methionyl-Trnafmet within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg584 b:45.9 occ:1.00 OP2 C:G9 2.7 77.7 1.0 OP1 C:4SU8 3.3 72.0 1.0 OP1 C:G9 3.5 74.8 1.0 P C:G9 3.5 72.7 1.0 OP2 C:A11 3.8 46.0 1.0 O5' C:G9 4.2 73.7 1.0 C5' C:4SU8 4.2 68.0 1.0 O5' C:4SU8 4.3 70.5 1.0 P C:4SU8 4.4 70.0 1.0 OP1 C:A11 4.6 55.8 1.0 OP2 C:G10 4.7 56.4 1.0 P C:A11 4.8 55.7 1.0 O3' C:4SU8 4.9 69.7 1.0

Magnesium binding site 2 out of 2 in the Methionyl-Trnafmet Formyltransferase Complexed with Formyl- Methionyl-Trnafmet


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Methionyl-Trnafmet Formyltransferase Complexed with Formyl- Methionyl-Trnafmet within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg585 b:39.4 occ:1.00 OP2 D:G9 2.7 77.8 1.0 OP1 D:G9 3.0 79.6 1.0 P D:G9 3.3 80.0 1.0 OP1 D:4SU8 3.5 71.4 1.0 OP2 D:A11 3.8 55.0 1.0 O5' D:G9 4.0 74.9 1.0 OP2 D:G10 4.3 61.8 1.0 C5' D:4SU8 4.4 74.2 1.0 O5' D:4SU8 4.4 74.4 1.0 OP1 D:A11 4.5 54.2 1.0 P D:4SU8 4.6 74.0 1.0 O3' D:4SU8 4.7 77.3 1.0 P D:A11 4.7 54.4 1.0

E.Schmitt, M.Panvert, S.Blanquet, Y.Mechulam. Crystal Structure of Methionyl-Trnafmet Transformylase Complexed with the Initiator Formyl-Methionyl-Trnafmet. Embo J. V. 17 6819 1998.
ISSN: ISSN 0261-4189
PubMed: 9843487
DOI: 10.1093/EMBOJ/17.23.6819