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Magnesium in PDB 3noj: The Structure of Hmg/Cha Aldolase From the Protocatechuate Degradation Pathway of Pseudomonas Putida

Enzymatic activity of The Structure of Hmg/Cha Aldolase From the Protocatechuate Degradation Pathway of Pseudomonas Putida

All present enzymatic activity of The Structure of Hmg/Cha Aldolase From the Protocatechuate Degradation Pathway of Pseudomonas Putida:
4.1.3.17;

Protein crystallography data

The structure of The Structure of Hmg/Cha Aldolase From the Protocatechuate Degradation Pathway of Pseudomonas Putida, PDB code: 3noj was solved by M.S.Kimber, W.Wang, S.Mazurkewich, S.Y.K.Seah, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.22 / 1.82
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 111.180, 111.180, 139.273, 90.00, 90.00, 120.00
R / Rfree (%) 15.9 / 17.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The Structure of Hmg/Cha Aldolase From the Protocatechuate Degradation Pathway of Pseudomonas Putida (pdb code 3noj). 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 Structure of Hmg/Cha Aldolase From the Protocatechuate Degradation Pathway of Pseudomonas Putida, PDB code: 3noj:

Magnesium binding site 1 out of 1 in 3noj

Go back to Magnesium Binding Sites List in 3noj
Magnesium binding site 1 out of 1 in the The Structure of Hmg/Cha Aldolase From the Protocatechuate Degradation Pathway of Pseudomonas Putida


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Structure of Hmg/Cha Aldolase From the Protocatechuate Degradation Pathway of Pseudomonas Putida within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg239

b:24.5
occ:1.00
 O A:HOH243 2.0 24.2 1.0
O A:HOH343 2.1 26.6 1.0
O3 A:PYR240 2.1 25.0 1.0
OD2 A:ASP124 2.1 24.8 1.0
O A:HOH258 2.1 27.1 1.0
O2 A:PYR240 2.1 27.5 1.0
C2 A:PYR240 2.8 26.7 1.0
C1 A:PYR240 2.9 26.8 1.0
CG A:ASP124 3.1 25.0 1.0
OD1 A:ASP124 3.4 25.9 1.0
N A:ASP102 4.1 25.9 1.0
NE A:ARG123 4.1 24.8 1.0
O1 A:PYR240 4.1 26.3 1.0
OD1 A:ASP102 4.2 37.8 1.0
C3 A:PYR240 4.3 24.3 1.0
CA A:GLY101 4.3 25.0 1.0
NH2 A:ARG123 4.3 27.2 1.0
OD2 A:ASP102 4.4 38.6 1.0
CG A:ASP102 4.4 32.9 1.0
CB A:ASP124 4.4 23.9 1.0
C A:GLY101 4.6 24.9 1.0
CZ A:ARG123 4.6 25.6 1.0
N A:LEU103 4.8 27.7 1.0
CG A:ARG123 4.9 23.0 1.0
CG A:LEU103 4.9 31.5 1.0
CD1 A:LEU103 4.9 34.7 1.0
N A:GLY101 4.9 24.7 1.0

Reference:

W.Wang, S.Mazurkewich, M.S.Kimber, S.Y.Seah. Structural and Kinetic Characterization of 4-Hydroxy-4-Methyl-2-Oxoglutarate/4-Carboxy-4-Hydroxy-2- Oxoadipate Aldolase, A Protocatechuate Degradation Enzyme Evolutionarily Convergent with the Hpai and Dmpg Pyruvate Aldolases. J.Biol.Chem. V. 285 36608 2010.
ISSN: ISSN 0021-9258
PubMed: 20843800
DOI: 10.1074/JBC.M110.159509
Page generated: Thu Aug 15 08:05:57 2024

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