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Magnesium in PDB 4lrs: Crystal and Solution Structures of the Bifunctional Enzyme (Aldolase/Aldehyde Dehydrogenase) From Thermomonospora Curvata, Reveal A Cofactor-Binding Domain Motion During Nad+ and Coa Accommodation Whithin the Shared Cofactor-Binding Site

Enzymatic activity of Crystal and Solution Structures of the Bifunctional Enzyme (Aldolase/Aldehyde Dehydrogenase) From Thermomonospora Curvata, Reveal A Cofactor-Binding Domain Motion During Nad+ and Coa Accommodation Whithin the Shared Cofactor-Binding Site

All present enzymatic activity of Crystal and Solution Structures of the Bifunctional Enzyme (Aldolase/Aldehyde Dehydrogenase) From Thermomonospora Curvata, Reveal A Cofactor-Binding Domain Motion During Nad+ and Coa Accommodation Whithin the Shared Cofactor-Binding Site:
1.2.1.10; 4.1.3.39;

Protein crystallography data

The structure of Crystal and Solution Structures of the Bifunctional Enzyme (Aldolase/Aldehyde Dehydrogenase) From Thermomonospora Curvata, Reveal A Cofactor-Binding Domain Motion During Nad+ and Coa Accommodation Whithin the Shared Cofactor-Binding Site, PDB code: 4lrs was solved by B.Fischer, G.Branlant, F.Talfournier, A.Gruez, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 1.55
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 149.880, 92.210, 56.480, 90.00, 100.59, 90.00
R / Rfree (%) 16.4 / 20

Other elements in 4lrs:

The structure of Crystal and Solution Structures of the Bifunctional Enzyme (Aldolase/Aldehyde Dehydrogenase) From Thermomonospora Curvata, Reveal A Cofactor-Binding Domain Motion During Nad+ and Coa Accommodation Whithin the Shared Cofactor-Binding Site also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal and Solution Structures of the Bifunctional Enzyme (Aldolase/Aldehyde Dehydrogenase) From Thermomonospora Curvata, Reveal A Cofactor-Binding Domain Motion During Nad+ and Coa Accommodation Whithin the Shared Cofactor-Binding Site (pdb code 4lrs). 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 and Solution Structures of the Bifunctional Enzyme (Aldolase/Aldehyde Dehydrogenase) From Thermomonospora Curvata, Reveal A Cofactor-Binding Domain Motion During Nad+ and Coa Accommodation Whithin the Shared Cofactor-Binding Site, PDB code: 4lrs:

Magnesium binding site 1 out of 1 in 4lrs

Go back to Magnesium Binding Sites List in 4lrs
Magnesium binding site 1 out of 1 in the Crystal and Solution Structures of the Bifunctional Enzyme (Aldolase/Aldehyde Dehydrogenase) From Thermomonospora Curvata, Reveal A Cofactor-Binding Domain Motion During Nad+ and Coa Accommodation Whithin the Shared Cofactor-Binding Site


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal and Solution Structures of the Bifunctional Enzyme (Aldolase/Aldehyde Dehydrogenase) From Thermomonospora Curvata, Reveal A Cofactor-Binding Domain Motion During Nad+ and Coa Accommodation Whithin the Shared Cofactor-Binding Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg404

b:9.0
occ:1.00
 O3 A:PYR402 2.0 16.7 1.0
O2 A:PYR402 2.1 20.7 1.0
NE2 A:HIS206 2.2 8.8 1.0
OD2 A:ASP22 2.2 11.1 1.0
NE2 A:HIS204 2.3 10.3 1.0
O A:HOH547 2.3 19.1 1.0
C2 A:PYR402 2.7 24.4 1.0
C1 A:PYR402 2.8 18.2 1.0
CE1 A:HIS206 3.1 9.8 1.0
CE1 A:HIS204 3.1 9.9 1.0
CG A:ASP22 3.2 9.7 1.0
CD2 A:HIS206 3.3 10.7 1.0
CD2 A:HIS204 3.3 10.4 1.0
OD1 A:ASP22 3.6 9.3 1.0
O1 A:PYR402 4.0 16.6 1.0
NH1 A:ARG21 4.1 8.8 1.0
O A:HOH584 4.1 24.9 1.0
ND2 A:ASN240 4.1 15.4 1.0
C3 A:PYR402 4.2 26.9 1.0
ND1 A:HIS204 4.3 9.3 1.0
ND1 A:HIS206 4.3 9.8 1.0
O A:HOH530 4.3 22.0 1.0
CG A:HIS206 4.4 9.6 1.0
CG A:HIS204 4.4 9.4 1.0
CB A:ASP22 4.5 8.7 1.0
NH2 A:ARG21 4.5 9.8 1.0
OG A:SER296 4.7 10.3 0.3
CZ A:ARG21 4.8 7.9 1.0
OD1 A:ASN240 4.9 14.8 1.0
CG A:ASN240 5.0 12.0 1.0

Reference:

B.Fischer, G.Branlant, F.Talfournier, A.Gruez. Crystal and Solution Structures of the Bifunctional Enzyme (Aldolase/Aldehyde Dehydrogenase) From Thermomonospora Curvata, Reveal A Cofactor-Binding Domain Motion During Nad+ and Coa Accommodation Whithin the Shared Cofactor-Binding Site To Be Published.
Page generated: Mon Dec 14 19:10:28 2020

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