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Aluminium in PDB 1tuy: Acetate Kinase Complexed with Adp, ALF3 and Acetate

Enzymatic activity of Acetate Kinase Complexed with Adp, ALF3 and Acetate

All present enzymatic activity of Acetate Kinase Complexed with Adp, ALF3 and Acetate:
2.7.2.1;

Protein crystallography data

The structure of Acetate Kinase Complexed with Adp, ALF3 and Acetate, PDB code: 1tuy was solved by A.Gorrell, S.H.Lawrence, J.G.Ferry, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.43 / 3.00
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 180.043, 67.196, 82.142, 90.00, 103.13, 90.00
R / Rfree (%) 20.1 / 26.3

Other elements in 1tuy:

The structure of Acetate Kinase Complexed with Adp, ALF3 and Acetate also contains other interesting chemical elements:

Fluorine (F) 3 atoms

Aluminium Binding Sites:

The binding sites of Aluminium atom in the Acetate Kinase Complexed with Adp, ALF3 and Acetate (pdb code 1tuy). This binding sites where shown within 5.0 Angstroms radius around Aluminium atom.
In total only one binding site of Aluminium was determined in the Acetate Kinase Complexed with Adp, ALF3 and Acetate, PDB code: 1tuy:

Aluminium binding site 1 out of 1 in 1tuy

Go back to Aluminium Binding Sites List in 1tuy
Aluminium binding site 1 out of 1 in the Acetate Kinase Complexed with Adp, ALF3 and Acetate


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Acetate Kinase Complexed with Adp, ALF3 and Acetate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Al448

b:44.8
occ:1.00
AL B:AF3448 0.0 44.8 1.0
F2 B:AF3448 1.8 43.0 1.0
F1 B:AF3448 1.9 42.6 1.0
F3 B:AF3448 1.9 40.0 1.0
N B:GLY212 4.0 7.0 1.0
CA B:GLY212 4.2 6.1 1.0
O B:ACY425 4.2 30.5 1.0
NE2 B:HIS180 4.3 7.8 1.0
O B:GLY212 4.5 7.2 1.0
CB B:ASN211 4.7 3.3 1.0
O1B B:ADP400 4.8 65.3 1.0
CH3 B:ACY425 4.8 30.6 1.0
C B:ASN211 4.8 6.9 1.0
C B:GLY212 4.9 6.7 1.0
N B:ASN211 5.0 4.3 1.0
C B:ACY425 5.0 30.6 1.0

Reference:

A.Gorrell, S.H.Lawrence, J.G.Ferry. Structural and Kinetic Analyses of Arginine Residues in the Active Site of the Acetate Kinase From Methanosarcina Thermophila. J.Biol.Chem. V. 280 10731 2005.
ISSN: ISSN 0021-9258
PubMed: 15647264
DOI: 10.1074/JBC.M412118200
Page generated: Wed Jul 10 09:26:31 2024

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