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Magnesium in PDB 4uhd: Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Acetate Bound)

Enzymatic activity of Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Acetate Bound)

All present enzymatic activity of Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Acetate Bound):
3.1.1.1;

Protein crystallography data

The structure of Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Acetate Bound), PDB code: 4uhd was solved by C.Sayer, M.N.Isupov, E.Bonch-Osmolovskaya, J.A.Littlechild, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 37.48 / 1.07
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 43.280, 43.280, 227.290, 90.00, 90.00, 120.00
R / Rfree (%) 9.351 / 11.203

Other elements in 4uhd:

The structure of Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Acetate Bound) also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Acetate Bound) (pdb code 4uhd). 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 Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Acetate Bound), PDB code: 4uhd:

Magnesium binding site 1 out of 1 in 4uhd

Go back to Magnesium Binding Sites List in 4uhd
Magnesium binding site 1 out of 1 in the Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Acetate Bound)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structural Studies of A Thermophilic Esterase From Thermogutta Terrifontis (Acetate Bound) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1277

b:12.6
occ:1.00
 O A:ILE237 2.3 11.0 1.0
OG A:SER240 2.3 11.3 1.0
O A:HOH2317 2.3 16.2 1.0
O A:HOH2316 2.4 20.1 1.0
O A:ALA234 2.4 11.8 1.0
O A:HOH2326 2.6 14.0 1.0
CB A:SER240 3.4 11.0 1.0
C A:ILE237 3.4 8.9 1.0
C A:ALA234 3.6 10.9 1.0
N A:ILE237 3.9 8.5 1.0
CA A:ARG235 4.1 13.1 0.3
CA A:ARG235 4.1 12.1 0.3
CA A:ARG235 4.1 11.4 0.3
C A:ARG235 4.1 10.8 1.0
N A:SER240 4.2 9.8 1.0
CA A:ILE237 4.2 8.4 1.0
O A:HOH2320 4.3 18.9 1.0
N A:ARG235 4.3 12.1 1.0
O A:ARG235 4.3 11.7 1.0
CA A:SER240 4.4 9.6 1.0
C A:PRO238 4.4 9.4 0.4
N A:PRO238 4.4 8.4 0.4
O A:PRO238 4.4 10.7 0.4
N A:PRO238 4.4 8.2 0.6
CA A:PRO238 4.5 10.1 0.4
O A:HOH2318 4.5 28.0 1.0
CB A:ILE237 4.5 9.8 1.0
N A:THR236 4.6 11.5 1.0
CA A:PRO238 4.6 9.0 0.6
NH1 A:ARG235 4.6 21.9 0.3
CA A:ALA234 4.7 11.2 1.0
C A:PRO238 4.8 8.0 0.6
C A:THR236 4.8 8.6 1.0
N A:GLN239 4.9 10.2 0.4
O A:SER240 4.9 10.9 1.0
N A:GLN239 5.0 8.5 0.6
CB A:ALA234 5.0 12.3 1.0

Reference:

C.Sayer, M.N.Isupov, E.Bonch-Osmolovskaya, J.A.Littlechild. Structural Studies of A Thermophilic Esterase From A New Planctomycetes Species, Thermogutta Terrifontis. Febs J. V. 282 2846 2015.
ISSN: ISSN 1742-464X
PubMed: 26011036
DOI: 10.1111/FEBS.13326
Page generated: Tue Aug 20 04:43:14 2024

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