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Yttrium in PDB 1rvg: Crystal Strcuture of Class II Fructose-Bisphosphate Aldolase From Thermus Aquaticus in Complex with Y

Enzymatic activity of Crystal Strcuture of Class II Fructose-Bisphosphate Aldolase From Thermus Aquaticus in Complex with Y

All present enzymatic activity of Crystal Strcuture of Class II Fructose-Bisphosphate Aldolase From Thermus Aquaticus in Complex with Y:
4.1.2.13;

Protein crystallography data

The structure of Crystal Strcuture of Class II Fructose-Bisphosphate Aldolase From Thermus Aquaticus in Complex with Y, PDB code: 1rvg was solved by T.Izard, J.Sygusch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.00 / 2.00
Space group P 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 99.860, 57.550, 138.617, 90.00, 90.26, 90.00
R / Rfree (%) 22.5 / 25.9

Other elements in 1rvg:

The structure of Crystal Strcuture of Class II Fructose-Bisphosphate Aldolase From Thermus Aquaticus in Complex with Y also contains other interesting chemical elements:

Cobalt (Co) 5 atoms
Sodium (Na) 4 atoms

Yttrium Binding Sites:

The binding sites of Yttrium atom in the Crystal Strcuture of Class II Fructose-Bisphosphate Aldolase From Thermus Aquaticus in Complex with Y (pdb code 1rvg). This binding sites where shown within 5.0 Angstroms radius around Yttrium atom.
In total only one binding site of Yttrium was determined in the Crystal Strcuture of Class II Fructose-Bisphosphate Aldolase From Thermus Aquaticus in Complex with Y, PDB code: 1rvg:

Yttrium binding site 1 out of 1 in 1rvg

Go back to Yttrium Binding Sites List in 1rvg
Yttrium binding site 1 out of 1 in the Crystal Strcuture of Class II Fructose-Bisphosphate Aldolase From Thermus Aquaticus in Complex with Y


Mono view


Stereo pair view

A full contact list of Yttrium with other atoms in the Y binding site number 1 of Crystal Strcuture of Class II Fructose-Bisphosphate Aldolase From Thermus Aquaticus in Complex with Y within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Y1801

b:39.9
occ:1.00
 OD1 A:ASP102 2.7 26.1 1.0
OD2 A:ASP102 2.7 26.3 1.0
OG A:SER104 2.8 28.9 1.0
OE2 A:GLU132 2.9 25.6 0.5
OE2 A:GLU132 2.9 27.1 0.5
O A:HOH1964 2.9 41.1 1.0
CG A:ASP102 3.0 26.3 1.0
O2 A:SO41609 3.2 56.4 1.0
O1 A:SO41609 3.3 56.4 1.0
O3 A:SO41609 3.4 56.2 1.0
S A:SO41609 3.5 56.3 1.0
CD A:GLU132 3.6 25.8 0.5
CD A:GLU132 3.7 26.7 0.5
OE1 A:GLU132 3.8 26.1 0.5
OE1 A:GLU132 4.0 26.7 0.5
CB A:SER104 4.0 29.4 1.0
CE1 A:HIS81 4.2 22.6 0.5
ND1 A:HIS81 4.4 22.6 0.5
CB A:ASP102 4.5 26.3 1.0
N A:SER104 4.6 28.8 1.0
O A:HOH2006 4.7 46.1 1.0
CG A:GLU132 4.8 26.4 0.5
CG A:GLU132 4.8 25.8 0.5
CA A:SER104 4.8 29.4 1.0
ND1 A:HIS105 4.9 30.0 1.0
O4 A:SO41609 5.0 56.7 1.0

Reference:

T.Izard, J.Sygusch. Induced Fit Movements and Metal Cofactor Selectivity of Class II Aldolases: Structure of Thermus Aquaticus Fructose-1,6-Bisphosphate Aldolase. J.Biol.Chem. V. 279 11825 2004.
ISSN: ISSN 0021-9258
PubMed: 14699122
DOI: 10.1074/JBC.M311375200
Page generated: Sat Oct 12 20:24:35 2024

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