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Manganese in PDB 1ylh: Crystal Structure of Phosphoenolpyruvate Carboxykinase From Actinobaccilus Succinogenes in Complex with Manganese and Pyruvate

Enzymatic activity of Crystal Structure of Phosphoenolpyruvate Carboxykinase From Actinobaccilus Succinogenes in Complex with Manganese and Pyruvate

All present enzymatic activity of Crystal Structure of Phosphoenolpyruvate Carboxykinase From Actinobaccilus Succinogenes in Complex with Manganese and Pyruvate:
4.1.1.49;

Protein crystallography data

The structure of Crystal Structure of Phosphoenolpyruvate Carboxykinase From Actinobaccilus Succinogenes in Complex with Manganese and Pyruvate, PDB code: 1ylh was solved by Y.A.Leduc, L.Prasad, M.Laivenieks, J.G.Zeikus, L.T.Delbaere, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.26 / 1.70
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 56.737, 55.089, 90.077, 90.00, 106.17, 90.00
R / Rfree (%) 19 / 21.5

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Phosphoenolpyruvate Carboxykinase From Actinobaccilus Succinogenes in Complex with Manganese and Pyruvate (pdb code 1ylh). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of Phosphoenolpyruvate Carboxykinase From Actinobaccilus Succinogenes in Complex with Manganese and Pyruvate, PDB code: 1ylh:

Manganese binding site 1 out of 1 in 1ylh

Go back to Manganese Binding Sites List in 1ylh
Manganese binding site 1 out of 1 in the Crystal Structure of Phosphoenolpyruvate Carboxykinase From Actinobaccilus Succinogenes in Complex with Manganese and Pyruvate


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Phosphoenolpyruvate Carboxykinase From Actinobaccilus Succinogenes in Complex with Manganese and Pyruvate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn560

b:15.9
occ:1.00
 O A:HOH864 2.2 20.5 1.0
NE2 A:HIS232 2.2 12.4 1.0
NZ A:LYS213 2.3 16.2 1.0
OD1 A:ASP269 2.4 20.0 1.0
O A:HOH753 2.4 29.0 1.0
O A:HOH863 2.4 32.0 1.0
OD2 A:ASP269 2.6 17.1 1.0
CG A:ASP269 2.8 15.9 1.0
CE1 A:HIS232 3.2 16.4 1.0
CE A:LYS213 3.2 16.7 1.0
CD2 A:HIS232 3.2 13.9 1.0
CB A:ASP269 4.3 14.6 1.0
ND1 A:HIS232 4.3 12.7 1.0
CG A:HIS232 4.4 13.0 1.0
O A:HOH796 4.5 31.1 1.0
CE A:LYS212 4.5 20.6 1.0
CD A:LYS213 4.6 15.3 1.0
O3 A:PYR931 4.6 35.5 1.0
O2 A:PYR931 4.7 27.7 1.0
NZ A:LYS212 4.8 20.4 1.0
CE2 A:PHE413 4.8 14.2 1.0
O A:ASP269 4.9 12.9 1.0
C2 A:PYR931 5.0 34.0 1.0

Reference:

Y.A.Leduc, L.Prasad, M.Laivenieks, J.G.Zeikus, L.T.Delbaere. Structure of Pep Carboxykinase From the Succinate-Producing Actinobacillus Succinogenes: A New Conserved Active-Site Motif. Acta Crystallogr.,Sect.D V. 61 903 2005.
ISSN: ISSN 0907-4449
PubMed: 15983413
DOI: 10.1107/S0907444905008723
Page generated: Sat Oct 5 13:12:33 2024

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