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Magnesium in PDB 6sll: Diaminobutyrate Acetyltransferase Ecta From Paenibacillus Lautus in Complex with Its Substrate L-2,4-Diaminobutyric Acid (Dab) and Coenzyme A

Enzymatic activity of Diaminobutyrate Acetyltransferase Ecta From Paenibacillus Lautus in Complex with Its Substrate L-2,4-Diaminobutyric Acid (Dab) and Coenzyme A

All present enzymatic activity of Diaminobutyrate Acetyltransferase Ecta From Paenibacillus Lautus in Complex with Its Substrate L-2,4-Diaminobutyric Acid (Dab) and Coenzyme A:
2.3.1.178;

Protein crystallography data

The structure of Diaminobutyrate Acetyltransferase Ecta From Paenibacillus Lautus in Complex with Its Substrate L-2,4-Diaminobutyric Acid (Dab) and Coenzyme A, PDB code: 6sll was solved by A.A.Richter, S.Kobus, L.Czech, A.Hoeppner, E.Bremer, S.H.J.Smits, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 75.52 / 1.20
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 151.048, 151.048, 46.172, 90.00, 90.00, 120.00
R / Rfree (%) 12.2 / 15

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Diaminobutyrate Acetyltransferase Ecta From Paenibacillus Lautus in Complex with Its Substrate L-2,4-Diaminobutyric Acid (Dab) and Coenzyme A (pdb code 6sll). 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 Diaminobutyrate Acetyltransferase Ecta From Paenibacillus Lautus in Complex with Its Substrate L-2,4-Diaminobutyric Acid (Dab) and Coenzyme A, PDB code: 6sll:

Magnesium binding site 1 out of 1 in 6sll

Go back to Magnesium Binding Sites List in 6sll
Magnesium binding site 1 out of 1 in the Diaminobutyrate Acetyltransferase Ecta From Paenibacillus Lautus in Complex with Its Substrate L-2,4-Diaminobutyric Acid (Dab) and Coenzyme A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Diaminobutyrate Acetyltransferase Ecta From Paenibacillus Lautus in Complex with Its Substrate L-2,4-Diaminobutyric Acid (Dab) and Coenzyme A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg203

b:34.1
occ:1.00
 O A:VAL116 2.8 11.9 1.0
O A:HOH563 3.0 37.9 1.0
NH1 A:ARG124 3.4 32.4 1.0
CA A:PRO118 3.5 14.0 1.0
N A:PRO118 3.7 12.9 1.0
C A:SER117 3.7 12.1 1.0
CZ A:PHE161 3.8 19.6 1.0
O A:SER117 3.8 13.3 1.0
CE1 A:PHE161 3.8 15.1 1.0
C A:VAL116 3.9 10.4 1.0
CD A:ARG124 3.9 23.4 1.0
CG A:PRO159 4.0 16.5 1.0
CB A:PRO118 4.2 17.9 1.0
CZ A:ARG124 4.3 25.5 1.0
CD A:PRO118 4.4 13.1 1.0
O A:HOH566 4.4 43.9 1.0
CG1 A:VAL116 4.4 14.8 1.0
CB A:VAL116 4.4 11.6 1.0
NE A:ARG124 4.5 24.5 1.0
CA A:SER117 4.5 11.6 1.0
C A:PRO118 4.6 14.7 1.0
N A:SER117 4.6 11.2 1.0
O A:PRO118 4.7 16.9 1.0
CG A:PRO118 4.7 17.8 1.0
CD A:PRO159 4.8 12.2 1.0
CA A:VAL116 4.8 10.5 1.0
O A:HOH517 4.9 30.9 1.0
O A:HOH569 4.9 52.6 1.0

Reference:

A.Richter, S.Kobus, L.Czech, A.Hoeppner, J.Zarzycki, T.Erb, L.Lauterbach, J.S.Dickschat, E.Bremer, S.H.J.Smits. The Architecture of the Diaminobutyrate Acetyltransferase Active Site Provides Mechanistic Insight Into the Biosynthesis of the Chemical Chaperone Ectoine J.Biol.Chem. 2020.
ISSN: ESSN 1083-351X
Page generated: Tue Oct 1 18:00:13 2024

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