Magnesium in PDB 6ojw: Crystal Structure of Sphingomonas Paucimobilis TMY1009 Holo-Lsda

Enzymatic activity of Crystal Structure of Sphingomonas Paucimobilis TMY1009 Holo-Lsda

All present enzymatic activity of Crystal Structure of Sphingomonas Paucimobilis TMY1009 Holo-Lsda:
1.13.11.43;

Protein crystallography data

The structure of Crystal Structure of Sphingomonas Paucimobilis TMY1009 Holo-Lsda, PDB code: 6ojw was solved by E.Kuatsjah, M.M.Verstraete, M.J.Kobylarz, A.K.N.Liu, M.E.P.Murphy, L.D.Eltis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 79.35 / 2.60
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 183.259, 183.259, 95.081, 90.00, 90.00, 120.00
R / Rfree (%) 18.7 / 21.5

Other elements in 6ojw:

The structure of Crystal Structure of Sphingomonas Paucimobilis TMY1009 Holo-Lsda also contains other interesting chemical elements:

Iron (Fe) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Sphingomonas Paucimobilis TMY1009 Holo-Lsda (pdb code 6ojw). 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 Sphingomonas Paucimobilis TMY1009 Holo-Lsda, PDB code: 6ojw:

Magnesium binding site 1 out of 1 in 6ojw

Go back to Magnesium Binding Sites List in 6ojw
Magnesium binding site 1 out of 1 in the Crystal Structure of Sphingomonas Paucimobilis TMY1009 Holo-Lsda


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 Sphingomonas Paucimobilis TMY1009 Holo-Lsda within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg502

b:36.0
occ:1.00
HH12 B:ARG15 2.2 38.9 1.0
HB3 A:LYS462 2.3 30.7 1.0
O A:LEU463 2.7 29.1 1.0
HB3 A:TYR442 2.8 34.7 1.0
NH1 B:ARG15 3.1 32.4 1.0
HA A:LYS462 3.1 32.3 1.0
OD1 A:ASP444 3.1 36.4 1.0
CB A:LYS462 3.2 25.6 1.0
H A:LEU463 3.2 33.8 1.0
HH22 B:ARG15 3.3 42.3 1.0
N A:LEU463 3.3 28.1 1.0
C A:LYS462 3.3 28.2 1.0
CA A:LYS462 3.4 26.9 1.0
HH11 B:ARG15 3.5 38.9 1.0
C A:LEU463 3.6 30.6 1.0
CB A:TYR442 3.7 28.9 1.0
O A:SER443 3.8 28.1 1.0
HB2 A:LYS462 3.8 30.7 1.0
NH2 B:ARG15 3.9 35.2 1.0
CZ B:ARG15 3.9 37.7 1.0
HG2 A:LYS462 4.0 38.1 1.0
CG A:TYR442 4.0 26.6 1.0
HB2 A:TYR442 4.0 34.7 1.0
CA A:LEU463 4.0 28.9 1.0
O A:LYS462 4.1 31.6 1.0
HD2 A:LYS462 4.1 40.9 1.0
CG A:LYS462 4.1 31.7 1.0
CG A:ASP444 4.3 31.6 1.0
HA A:PRO464 4.3 34.7 1.0
H A:SER443 4.3 40.1 1.0
CD2 A:TYR442 4.4 29.2 1.0
HD2 A:TYR442 4.4 35.1 1.0
CD1 A:TYR442 4.5 27.2 1.0
C A:SER443 4.5 30.2 1.0
N A:PRO464 4.6 31.1 1.0
N A:SER443 4.6 33.4 1.0
HD1 A:TYR442 4.6 32.6 1.0
CD A:LYS462 4.6 34.1 1.0
HH21 B:ARG15 4.7 42.3 1.0
HA A:LEU463 4.7 34.6 1.0
HB2 A:LEU463 4.7 35.1 1.0
CA A:TYR442 4.8 29.8 1.0
N A:LYS462 4.8 32.1 1.0
HA A:ASP444 4.8 36.0 1.0
HA A:TYR442 4.9 35.8 1.0
OD2 A:ASP444 4.9 30.5 1.0
C A:TYR442 4.9 31.1 1.0
HG3 A:LYS462 5.0 38.1 1.0
CA A:PRO464 5.0 28.9 1.0

Reference:

E.Kuatsjah, M.M.Verstraete, M.J.Kobylarz, A.K.N.Liu, M.E.P.Murphy, L.D.Eltis. Identification of Functionally Important Residues and Structural Features in A Bacterial Lignostilbene Dioxygenase. J.Biol.Chem. V. 294 12911 2019.
ISSN: ESSN 1083-351X
PubMed: 31292192
DOI: 10.1074/JBC.RA119.009428
Page generated: Mon Dec 14 23:43:34 2020

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