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Magnesium in PDB 2plj: Crystal Structure of Lysine/Ornithine Decarboxylase Complexed with Putrescine From Vibrio Vulnificus

Enzymatic activity of Crystal Structure of Lysine/Ornithine Decarboxylase Complexed with Putrescine From Vibrio Vulnificus

All present enzymatic activity of Crystal Structure of Lysine/Ornithine Decarboxylase Complexed with Putrescine From Vibrio Vulnificus:
4.1.1.17; 4.1.1.18;

Protein crystallography data

The structure of Crystal Structure of Lysine/Ornithine Decarboxylase Complexed with Putrescine From Vibrio Vulnificus, PDB code: 2plj was solved by J.Lee, E.J.Goldsmith, M.A.Phillips, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.72 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 82.074, 88.683, 111.843, 90.00, 90.00, 90.00
R / Rfree (%) 18.1 / 21.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Lysine/Ornithine Decarboxylase Complexed with Putrescine From Vibrio Vulnificus (pdb code 2plj). 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 Lysine/Ornithine Decarboxylase Complexed with Putrescine From Vibrio Vulnificus, PDB code: 2plj:

Magnesium binding site 1 out of 1 in 2plj

Go back to Magnesium Binding Sites List in 2plj
Magnesium binding site 1 out of 1 in the Crystal Structure of Lysine/Ornithine Decarboxylase Complexed with Putrescine From Vibrio Vulnificus


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 Lysine/Ornithine Decarboxylase Complexed with Putrescine From Vibrio Vulnificus within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg400

b:38.9
occ:1.00
 O A:HOH750 2.0 35.0 1.0
O A:HOH742 2.2 34.6 1.0
O A:HOH800 2.2 36.6 1.0
O A:HOH576 2.2 26.5 1.0
O A:HOH802 2.2 38.4 1.0
O A:HOH801 2.4 39.7 1.0
OD1 A:ASN126 3.9 23.0 1.0
OE2 A:GLU147 4.1 24.0 1.0
O A:HOH537 4.4 21.6 1.0
O A:HOH577 4.4 25.0 1.0
O A:HOH709 4.5 37.6 1.0
O A:HOH570 4.5 27.2 1.0
O A:ASP103 4.6 17.9 1.0
CG2 A:VAL127 4.6 15.8 1.0
CG A:ASN126 4.8 20.9 1.0
ND2 A:ASN126 4.8 29.2 1.0
CB A:ASP103 4.9 17.9 1.0
CA A:ASP103 4.9 16.8 1.0
NZ A:LYS189 4.9 23.4 1.0

Reference:

J.Lee, A.J.Michael, D.Martynowski, E.J.Goldsmith, M.A.Phillips. Phylogenetic Diversity and the Structural Basis of Substrate Specificity in the Beta/Alpha-Barrel Fold Basic Amino Acid Decarboxylases. J.Biol.Chem. V. 282 27115 2007.
ISSN: ISSN 0021-9258
PubMed: 17626020
DOI: 10.1074/JBC.M704066200
Page generated: Wed Aug 14 02:09:44 2024

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