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Magnesium in PDB 4lrt: 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: 4lrt 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) 46.45 / 1.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 94.500, 116.700, 131.500, 90.00, 90.00, 90.00
R / Rfree (%) 15.1 / 17

Other elements in 4lrt:

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:

Sodium (Na) 4 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 4lrt). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where 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: 4lrt:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 4lrt

Go back to Magnesium Binding Sites List in 4lrt
Magnesium binding site 1 out of 2 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:Mg403

b:9.2
occ:1.00
 O3 A:PYR401 2.0 20.8 0.7
OD1 A:ASP22 2.1 18.9 1.0
O2 A:PYR401 2.1 17.9 0.7
O A:HOH543 2.2 21.1 1.0
NE2 A:HIS206 2.3 16.9 1.0
NE2 A:HIS204 2.3 17.8 1.0
C2 A:PYR401 2.8 21.6 0.7
C1 A:PYR401 2.8 18.2 0.7
CE1 A:HIS206 3.1 15.9 1.0
CG A:ASP22 3.1 17.2 1.0
CE1 A:HIS204 3.2 17.6 1.0
CD2 A:HIS204 3.3 17.8 1.0
CD2 A:HIS206 3.3 17.6 1.0
OD2 A:ASP22 3.5 18.3 1.0
O A:HOH857 4.1 24.2 1.0
NH2 A:ARG21 4.1 14.8 1.0
O1 A:PYR401 4.1 13.8 0.7
ND2 A:ASN240 4.2 21.2 1.0
C3 A:PYR401 4.3 25.5 0.7
ND1 A:HIS206 4.3 16.8 1.0
ND1 A:HIS204 4.3 15.8 1.0
O A:HOH595 4.3 26.3 1.0
CG A:HIS204 4.4 14.9 1.0
CB A:ASP22 4.4 13.6 1.0
CG A:HIS206 4.4 16.3 1.0
NH1 A:ARG21 4.5 13.9 1.0
CZ A:ARG21 4.7 13.4 1.0
OD1 A:ASN240 4.9 22.8 1.0
CG A:ASN240 5.0 19.9 1.0

Magnesium binding site 2 out of 2 in 4lrt

Go back to Magnesium Binding Sites List in 4lrt
Magnesium binding site 2 out of 2 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 2 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
C:Mg404

b:8.6
occ:1.00
 O3 C:PYR401 2.0 18.7 0.7
O2 C:PYR401 2.1 18.0 0.7
OD2 C:ASP22 2.1 17.8 1.0
NE2 C:HIS206 2.2 15.7 1.0
NE2 C:HIS204 2.2 16.8 1.0
O C:HOH567 2.3 21.2 1.0
C2 C:PYR401 2.8 18.7 0.7
C1 C:PYR401 2.8 16.5 0.7
CE1 C:HIS206 3.1 17.2 1.0
CE1 C:HIS204 3.1 18.7 1.0
CG C:ASP22 3.1 16.8 1.0
CD2 C:HIS204 3.3 16.6 1.0
CD2 C:HIS206 3.3 17.0 1.0
OD1 C:ASP22 3.5 17.4 1.0
O C:HOH866 4.0 22.0 1.0
O1 C:PYR401 4.1 15.2 0.7
NH2 C:ARG21 4.1 15.1 1.0
ND2 C:ASN240 4.3 22.1 1.0
ND1 C:HIS204 4.3 16.7 1.0
ND1 C:HIS206 4.3 16.1 1.0
O C:HOH574 4.3 25.2 1.0
C3 C:PYR401 4.3 22.8 0.7
CG C:HIS204 4.4 13.8 1.0
CG C:HIS206 4.4 15.7 1.0
CB C:ASP22 4.4 13.5 1.0
NH1 C:ARG21 4.5 13.3 1.0
CZ C:ARG21 4.8 13.5 1.0
OD1 C:ASN240 4.9 23.9 1.0
CG C:ASN240 5.0 20.3 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 Aug 19 20:03:12 2024

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