Magnesium in PDB 6a00: The Crystal Structure of Mandelate Oxidase with (S)-2-Phenylpropionate

Enzymatic activity of The Crystal Structure of Mandelate Oxidase with (S)-2-Phenylpropionate

All present enzymatic activity of The Crystal Structure of Mandelate Oxidase with (S)-2-Phenylpropionate:
1.1.3.46;

Protein crystallography data

The structure of The Crystal Structure of Mandelate Oxidase with (S)-2-Phenylpropionate, PDB code: 6a00 was solved by T.L.Li, K.H.Lin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.38 / 1.59
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 138.194, 138.194, 111.699, 90.00, 90.00, 90.00
R / Rfree (%) 17.4 / 19

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Crystal Structure of Mandelate Oxidase with (S)-2-Phenylpropionate (pdb code 6a00). 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 The Crystal Structure of Mandelate Oxidase with (S)-2-Phenylpropionate, PDB code: 6a00:

Magnesium binding site 1 out of 1 in 6a00

Go back to Magnesium Binding Sites List in 6a00
Magnesium binding site 1 out of 1 in the The Crystal Structure of Mandelate Oxidase with (S)-2-Phenylpropionate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Crystal Structure of Mandelate Oxidase with (S)-2-Phenylpropionate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:16.3
occ:1.00
O3P A:FMN402 2.7 9.8 1.0
O A:LEU304 2.8 9.7 1.0
N A:GLY284 2.9 7.7 1.0
N A:ILE286 3.2 8.5 1.0
CG1 A:ILE286 3.4 8.5 1.0
CB A:ILE286 3.4 9.9 1.0
N A:GLY285 3.4 8.7 1.0
C A:GLY284 3.6 10.9 1.0
CA A:GLY284 3.6 9.9 1.0
P A:FMN402 3.7 11.0 1.0
C A:ASP283 3.8 9.6 1.0
CA A:ILE286 3.9 10.3 1.0
CA A:ASP283 3.9 8.2 1.0
O5' A:FMN402 3.9 20.9 1.0
CB A:ASP283 3.9 7.5 1.0
C A:LEU304 3.9 8.7 1.0
CA A:VAL305 4.0 7.6 1.0
O2P A:FMN402 4.0 12.1 1.0
C5' A:FMN402 4.1 12.2 1.0
C A:GLY285 4.2 10.2 1.0
O A:GLY284 4.2 11.3 1.0
NH1 A:ARG287 4.2 13.8 1.0
CA A:GLY285 4.3 11.2 1.0
O A:ILE286 4.3 11.4 1.0
N A:VAL305 4.4 7.3 1.0
N A:GLY306 4.5 8.0 1.0
C A:ILE286 4.6 10.8 1.0
CD1 A:ILE286 4.8 12.9 1.0
C A:VAL305 4.8 8.3 1.0
CG2 A:ILE286 4.8 13.8 1.0
CG2 A:VAL305 4.9 9.3 1.0
CG A:ASP283 4.9 9.6 1.0
CB A:VAL305 4.9 7.7 1.0
O A:ASP283 4.9 9.0 1.0

Reference:

H.W.Yeh, K.H.Lin, S.Y.Lyu, Y.S.Li, C.M.Huang, Y.L.Wang, H.W.Shih, N.S.Hsu, C.J.Wu, T.L.Li. Biochemical and Structural Explorations of Alpha-Hydroxyacid Oxidases Reveal A Four-Electron Oxidative Decarboxylation Reaction. Acta Crystallogr D Struct V. 75 733 2019BIOL.
ISSN: ISSN 2059-7983
PubMed: 31373572
DOI: 10.1107/S2059798319009574
Page generated: Mon Dec 14 22:18:36 2020

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