Magnesium in PDB 7wik: Crystal Structure of Oligoribonuclease of Mycobacterium Smegmatis MC2 155

Enzymatic activity of Crystal Structure of Oligoribonuclease of Mycobacterium Smegmatis MC2 155

All present enzymatic activity of Crystal Structure of Oligoribonuclease of Mycobacterium Smegmatis MC2 155:
3.1.13.3;

Protein crystallography data

The structure of Crystal Structure of Oligoribonuclease of Mycobacterium Smegmatis MC2 155, PDB code: 7wik was solved by P.Badhwar, B.Taneja, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 81.07 / 1.87
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 60.25, 97.26, 146.73, 90, 90, 90
R / Rfree (%) 17.9 / 22.2

Other elements in 7wik:

The structure of Crystal Structure of Oligoribonuclease of Mycobacterium Smegmatis MC2 155 also contains other interesting chemical elements:

Potassium (K) 4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Oligoribonuclease of Mycobacterium Smegmatis MC2 155 (pdb code 7wik). 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 Oligoribonuclease of Mycobacterium Smegmatis MC2 155, PDB code: 7wik:

Magnesium binding site 1 out of 1 in 7wik

Go back to Magnesium Binding Sites List in 7wik
Magnesium binding site 1 out of 1 in the Crystal Structure of Oligoribonuclease of Mycobacterium Smegmatis MC2 155


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 Oligoribonuclease of Mycobacterium Smegmatis MC2 155 within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mg310

b:40.9
occ:1.00
 OG C:SER66 2.5 25.2 1.0
ND1 C:HIS63 2.7 21.7 1.0
O C:HIS157 2.8 35.4 1.0
CB C:SER66 3.2 27.0 1.0
CE1 C:HIS63 3.4 22.7 1.0
O C:MET62 3.6 23.4 1.0
CA C:HIS63 3.6 24.1 1.0
CB C:HIS157 3.7 53.1 1.0
C C:HIS157 3.7 40.3 1.0
CD C:ARG158 3.9 38.1 1.0
CG C:HIS63 3.9 23.2 1.0
C C:MET62 3.9 23.6 1.0
N C:HIS63 4.0 23.3 1.0
CG C:MET62 4.0 39.6 1.0
CD2 C:LEU68 4.0 25.5 1.0
CB C:LEU68 4.1 23.8 1.0
CB C:HIS63 4.3 23.0 1.0
CA C:HIS157 4.3 47.7 1.0
CA C:SER66 4.6 26.5 1.0
O C:HOH475 4.6 37.2 1.0
C C:HIS63 4.6 24.3 1.0
CG C:ARG158 4.7 38.1 1.0
NE2 C:HIS63 4.7 20.5 1.0
O C:HIS63 4.7 23.6 1.0
CG C:LEU68 4.7 26.6 1.0
N C:ARG158 4.8 35.5 1.0
O C:ALA156 4.8 53.0 1.0
SD C:MET62 4.9 44.4 1.0
N C:SER66 4.9 26.4 1.0
CB C:MET62 4.9 31.2 1.0
CD2 C:HIS63 4.9 21.8 1.0
CG C:HIS157 4.9 65.1 1.0
CA C:MET62 5.0 26.9 1.0

Reference:

P.Badhwar, S.H.Khan, B.Taneja. Three-Dimensional Structure of A Mycobacterial Oligoribonuclease Reveals A Unique C-Terminal Tail That Stabilizes the Homodimer. J.Biol.Chem. V. 298 02595 2022.
ISSN: ESSN 1083-351X
PubMed: 36244449
DOI: 10.1016/J.JBC.2022.102595
Page generated: Fri Apr 7 01:50:16 2023

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