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Manganese in PDB 6btg: Crystal Structure of Deoxyribose-Phosphate Aldolase Bound with Dhap From Bacillus Thuringiensis

Enzymatic activity of Crystal Structure of Deoxyribose-Phosphate Aldolase Bound with Dhap From Bacillus Thuringiensis

All present enzymatic activity of Crystal Structure of Deoxyribose-Phosphate Aldolase Bound with Dhap From Bacillus Thuringiensis:
4.1.2.17;

Protein crystallography data

The structure of Crystal Structure of Deoxyribose-Phosphate Aldolase Bound with Dhap From Bacillus Thuringiensis, PDB code: 6btg was solved by Q.Li, S.D.Bruner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.98 / 1.70
Space group P 4 21 2
Cell size a, b, c (Å), α, β, γ (°) 105.104, 105.104, 49.366, 90.00, 90.00, 90.00
R / Rfree (%) 18.7 / 22.5

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Deoxyribose-Phosphate Aldolase Bound with Dhap From Bacillus Thuringiensis (pdb code 6btg). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of Deoxyribose-Phosphate Aldolase Bound with Dhap From Bacillus Thuringiensis, PDB code: 6btg:

Manganese binding site 1 out of 1 in 6btg

Go back to Manganese Binding Sites List in 6btg
Manganese binding site 1 out of 1 in the Crystal Structure of Deoxyribose-Phosphate Aldolase Bound with Dhap From Bacillus Thuringiensis


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Deoxyribose-Phosphate Aldolase Bound with Dhap From Bacillus Thuringiensis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn301

b:20.5
occ:1.00
 NE2 A:HIS157 2.1 17.5 1.0
NE2 A:HIS97 2.1 22.5 1.0
NE2 A:HIS95 2.1 20.1 1.0
O3 A:13P302 2.3 24.7 0.8
OE1 A:GLU76 2.4 16.5 0.5
O2 A:13P302 2.5 27.7 0.8
CE1 A:HIS97 3.0 22.8 1.0
CE1 A:HIS157 3.0 20.6 1.0
CD2 A:HIS157 3.1 20.4 1.0
CE1 A:HIS95 3.1 15.5 1.0
CD2 A:HIS97 3.1 19.8 1.0
CD2 A:HIS95 3.1 18.4 1.0
CD A:GLU76 3.2 19.3 0.5
OE2 A:GLU76 3.2 19.4 0.5
C2 A:13P302 3.2 26.1 0.8
C3 A:13P302 3.3 27.2 0.8
OE2 A:GLU76 4.1 18.1 0.5
ND1 A:HIS157 4.1 16.2 1.0
ND1 A:HIS97 4.2 25.8 1.0
CG A:HIS157 4.2 16.9 1.0
ND1 A:HIS95 4.2 18.7 1.0
CG A:HIS97 4.2 20.6 1.0
CG A:HIS95 4.3 16.2 1.0
N A:GLY28 4.4 20.4 1.0
CG A:GLU76 4.6 20.1 0.5
CG A:GLU76 4.6 20.2 0.5
CA A:GLY28 4.6 18.7 1.0
C1 A:13P302 4.7 27.3 0.8
CD A:GLU76 4.8 17.9 0.5
ND2 A:ASN29 4.8 20.5 1.0

Reference:

G.A.W.Beaudoin, Q.Li, J.Folz, O.Fiehn, J.L.Goodsell, A.Angerhofer, S.D.Bruner, A.D.Hanson. Salvage of the 5-Deoxyribose Byproduct of Radical Sam Enzymes. Nat Commun V. 9 3105 2018.
ISSN: ESSN 2041-1723
PubMed: 30082730
DOI: 10.1038/S41467-018-05589-4
Page generated: Sun Oct 6 03:57:02 2024

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