Magnesium in PDB 2x3j: Co-Complex Structure of Achromobactin Synthetase Protein D (Acsd) with Atp and N-Citryl-Ethylenediamine From Pectobacterium Chrysanthemi

The structure of Co-Complex Structure of Achromobactin Synthetase Protein D (Acsd) with Atp and N-Citryl-Ethylenediamine From Pectobacterium Chrysanthemi, PDB code: 2x3j was solved by S.Schmelz, G.L.Challis, J.H.Naismith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	92.85 / 2.00
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	57.704, 71.521, 95.595, 97.26, 101.97, 91.01
R / Rfree (%)	19 / 23.1

The binding sites of Magnesium atom in the Co-Complex Structure of Achromobactin Synthetase Protein D (Acsd) with Atp and N-Citryl-Ethylenediamine From Pectobacterium Chrysanthemi (pdb code 2x3j). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Co-Complex Structure of Achromobactin Synthetase Protein D (Acsd) with Atp and N-Citryl-Ethylenediamine From Pectobacterium Chrysanthemi, PDB code: 2x3j:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Co-Complex Structure of Achromobactin Synthetase Protein D (Acsd) with Atp and N-Citryl-Ethylenediamine From Pectobacterium Chrysanthemi


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Co-Complex Structure of Achromobactin Synthetase Protein D (Acsd) with Atp and N-Citryl-Ethylenediamine From Pectobacterium Chrysanthemi within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1590 b:37.2 occ:1.00 OD1 A:ASN447 2.1 26.6 1.0 O1G A:ATP1589 2.1 31.9 1.0 O1A A:ATP1589 2.2 38.3 1.0 OE1 A:GLN446 2.4 37.1 1.0 O3A A:ATP1589 2.4 37.9 1.0 OD1 A:ASP464 2.5 40.0 1.0 PA A:ATP1589 2.9 38.7 1.0 CG A:ASN447 3.2 29.0 1.0 PG A:ATP1589 3.3 34.0 1.0 CD A:GLN446 3.3 33.7 1.0 CG A:ASP464 3.4 38.5 1.0 PB A:ATP1589 3.5 37.0 1.0 NE2 A:GLN446 3.6 33.9 1.0 CB A:ASP464 3.6 37.1 1.0 O3B A:ATP1589 3.6 33.7 1.0 ND2 A:ASN447 3.7 27.9 1.0 O1B A:ATP1589 3.8 35.5 1.0 O3G A:ATP1589 3.8 30.5 1.0 O2A A:ATP1589 4.0 38.9 1.0 O5' A:ATP1589 4.0 38.4 1.0 CE1 A:HIS444 4.0 27.2 1.0 C5' A:ATP1589 4.1 39.0 1.0 O A:HOH2239 4.3 35.1 1.0 NE2 A:HIS444 4.4 23.9 1.0 CB A:ASN447 4.4 28.4 1.0 OD2 A:ASP464 4.5 39.9 1.0 O A:GLN446 4.5 28.6 1.0 CA A:ASN447 4.6 28.5 1.0 O2G A:ATP1589 4.6 33.8 1.0 N A:ASN447 4.7 28.2 1.0 CG A:GLN446 4.7 28.4 1.0 C A:GLN446 4.7 28.0 1.0 O2B A:ATP1589 4.8 35.1 1.0 C4' A:ATP1589 5.0 38.0 1.0

Magnesium binding site 2 out of 2 in the Co-Complex Structure of Achromobactin Synthetase Protein D (Acsd) with Atp and N-Citryl-Ethylenediamine From Pectobacterium Chrysanthemi


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Co-Complex Structure of Achromobactin Synthetase Protein D (Acsd) with Atp and N-Citryl-Ethylenediamine From Pectobacterium Chrysanthemi within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1589 b:34.4 occ:1.00 OD1 B:ASN447 2.1 29.0 1.0 O1G B:ATP1588 2.1 29.6 1.0 O1A B:ATP1588 2.2 35.5 1.0 OE1 B:GLN446 2.3 34.1 1.0 O3A B:ATP1588 2.4 33.4 1.0 OD1 B:ASP464 2.6 36.8 1.0 PA B:ATP1588 2.9 36.7 1.0 CD B:GLN446 3.2 33.4 1.0 CG B:ASN447 3.2 28.7 1.0 NE2 B:GLN446 3.4 35.1 1.0 PG B:ATP1588 3.4 28.7 1.0 CG B:ASP464 3.5 35.4 1.0 PB B:ATP1588 3.6 34.1 1.0 O3B B:ATP1588 3.7 30.1 1.0 CB B:ASP464 3.7 33.8 1.0 ND2 B:ASN447 3.8 26.6 1.0 O5' B:ATP1588 3.9 35.3 1.0 C5' B:ATP1588 4.0 35.5 1.0 O2B B:ATP1588 4.0 36.7 1.0 CE1 B:HIS444 4.0 26.9 1.0 O3G B:ATP1588 4.0 27.2 1.0 O2A B:ATP1588 4.2 35.8 1.0 O B:HOH2208 4.2 47.9 1.0 NE2 B:HIS444 4.3 25.3 1.0 CB B:ASN447 4.4 27.0 1.0 CA B:ASN447 4.5 26.7 1.0 O B:GLN446 4.5 27.9 1.0 O2G B:ATP1588 4.6 29.9 1.0 N B:ASN447 4.6 26.9 1.0 CG B:GLN446 4.6 29.6 1.0 OD2 B:ASP464 4.6 35.6 1.0 C B:GLN446 4.6 27.2 1.0 C4' B:ATP1588 4.7 35.1 1.0 O1B B:ATP1588 4.9 32.5 1.0 CB B:GLN446 5.0 27.3 1.0 O B:HOH2219 5.0 52.6 1.0

S.Schmelz, C.H.Botting, L.Song, N.F.Kadi, G.L.Challis, J.H.Naismith. Structural Basis For Acyl Acceptor Specificity in the Achromobactin Biosynthetic Enzyme Acsd. J.Mol.Biol. V. 412 495 2011.
ISSN: ISSN 0022-2836
PubMed: 21835184
DOI: 10.1016/J.JMB.2011.07.059