Magnesium in PDB 6tc9: Crystal Structure of Mutm From Neisseria Meningitidis

All present enzymatic activity of Crystal Structure of Mutm From Neisseria Meningitidis:
3.2.2.23; 4.2.99.18;

The structure of Crystal Structure of Mutm From Neisseria Meningitidis, PDB code: 6tc9 was solved by J.Silhan, B.Landova, E.Boura, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.22 / 2.18
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	130.770, 80.380, 83.620, 90.00, 89.95, 90.00
R / Rfree (%)	23.8 / 28.1

The structure of Crystal Structure of Mutm From Neisseria Meningitidis also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Magnesium atom in the Crystal Structure of Mutm From Neisseria Meningitidis (pdb code 6tc9). 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 Mutm From Neisseria Meningitidis, PDB code: 6tc9:

Magnesium binding site 1 out of 1 in the Crystal Structure of Mutm From Neisseria Meningitidis


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 Mutm From Neisseria Meningitidis within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg302 b:78.1 occ:1.00 CE1 A:TYR235 3.9 58.1 1.0 NE C:ARG214 3.9 74.8 1.0 CZ C:ARG214 3.9 79.0 1.0 NH1 C:ARG214 4.0 80.2 1.0 CD C:ARG214 4.1 68.7 1.0 NH2 C:ARG214 4.4 80.5 1.0 OH A:TYR235 4.4 64.3 1.0 CB C:ALA210 4.5 34.1 1.0 CZ A:TYR235 4.6 60.5 1.0 OE1 A:GLN237 4.6 83.8 1.0 CD1 A:TYR235 4.7 55.4 1.0 CZ C:ARG184 4.7 46.2 1.0 NE C:ARG184 4.7 43.6 1.0 C C:ALA210 4.8 41.5 1.0 CG A:GLN237 4.8 74.3 1.0 O C:ALA210 4.8 40.7 1.0 NH1 C:ARG184 4.9 44.8 1.0 CB C:ARG214 4.9 56.5 1.0 N C:VAL211 4.9 42.3 1.0 O A:HOH405 4.9 75.6 1.0 CD C:ARG184 4.9 41.7 1.0

B.Landova, J.Silhan. Conformational Changes of Dna Repair Glycosylase Mutm Triggered By Dna Binding. Febs Lett. 2020.
ISSN: ISSN 0014-5793
PubMed: 32598485
DOI: 10.1002/1873-3468.13876