Magnesium in PDB 6a08: The Crystal Structure of Mandelate Oxidase with Benzoyl-Formic Acid

Enzymatic activity of The Crystal Structure of Mandelate Oxidase with Benzoyl-Formic Acid

All present enzymatic activity of The Crystal Structure of Mandelate Oxidase with Benzoyl-Formic Acid:
1.1.3.46;

Protein crystallography data

The structure of The Crystal Structure of Mandelate Oxidase with Benzoyl-Formic Acid, PDB code: 6a08 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) 29.34 / 1.55
Space group I 4 2 2
Cell size a, b, c (Å), α, β, γ (°) 137.911, 137.911, 111.773, 90.00, 90.00, 90.00
R / Rfree (%) 16.4 / 18.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Crystal Structure of Mandelate Oxidase with Benzoyl-Formic Acid (pdb code 6a08). 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 Benzoyl-Formic Acid, PDB code: 6a08:

Magnesium binding site 1 out of 1 in 6a08

Go back to Magnesium Binding Sites List in 6a08
Magnesium binding site 1 out of 1 in the The Crystal Structure of Mandelate Oxidase with Benzoyl-Formic Acid


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 Benzoyl-Formic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:16.6
occ:1.00
O3P A:FMN402 2.7 9.9 1.0
O A:LEU304 2.8 8.7 1.0
N A:GLY284 2.9 7.5 1.0
N A:ILE286 3.2 7.9 1.0
CG1 A:ILE286 3.4 10.1 1.0
N A:GLY285 3.4 8.3 1.0
CB A:ILE286 3.4 10.5 1.0
C A:GLY284 3.6 9.8 1.0
P A:FMN402 3.6 10.3 1.0
O5' A:FMN402 3.6 14.8 1.0
CA A:GLY284 3.6 8.0 1.0
C A:ASP283 3.8 10.4 1.0
CA A:ILE286 3.9 8.2 1.0
C A:LEU304 3.9 7.6 1.0
CB A:ASP283 3.9 7.8 1.0
CA A:ASP283 3.9 7.7 1.0
O2P A:FMN402 3.9 11.4 1.0
CA A:VAL305 4.0 7.7 1.0
NH1 A:ARG287 4.1 12.2 1.0
C A:GLY285 4.2 9.2 1.0
O A:GLY284 4.3 11.1 1.0
O A:ILE286 4.3 12.4 1.0
CA A:GLY285 4.3 10.3 1.0
N A:VAL305 4.4 7.3 1.0
N A:GLY306 4.5 8.7 1.0
C A:ILE286 4.6 11.1 1.0
C5' A:FMN402 4.7 15.9 1.0
C A:VAL305 4.7 8.1 1.0
CD1 A:ILE286 4.8 13.8 1.0
CG2 A:VAL305 4.8 9.7 1.0
CG2 A:ILE286 4.8 13.5 1.0
CB A:VAL305 4.9 6.5 1.0
CG A:ASP283 4.9 12.4 1.0
O A:ASP283 5.0 10.2 1.0

Reference:

S.Y.Lyu, K.H.Lin, H.W.Yeh, Y.S.Li, C.M.Huang, Y.L.Wang, H.W.Shih, N.S.Hsu, C.J.Wu, T.L.Li. The Flavin Mononucleotide Cofactor in Alpha-Hydroxyacid Oxidases Exerts Its Electrophilic/Nucleophilic Duality in Control of the Substrate-Oxidation Level. Acta Crystallogr D Struct V. 75 918 2019BIOL.
ISSN: ISSN 2059-7983
PubMed: 31588923
DOI: 10.1107/S2059798319011938
Page generated: Mon Dec 14 22:18:36 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy