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Magnesium in PDB 2w02: Co-Complex Structure of Achromobactin Synthetase Protein D (Acsd) with Atp From Pectobacterium Chrysanthemi

Protein crystallography data

The structure of Co-Complex Structure of Achromobactin Synthetase Protein D (Acsd) with Atp From Pectobacterium Chrysanthemi, PDB code: 2w02 was solved by S.Schmelz, S.A.Mcmahon, N.Kadi, L.Song, D.Oves-Costales, M.Oke, H.Liu, K.A.Johnson, L.Carter, M.F.White, 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) 81.11 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 79.874, 94.542, 157.770, 90.00, 90.00, 90.00
R / Rfree (%) 21.6 / 27.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Co-Complex Structure of Achromobactin Synthetase Protein D (Acsd) with Atp From Pectobacterium Chrysanthemi (pdb code 2w02). 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 From Pectobacterium Chrysanthemi, PDB code: 2w02:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 2w02

Go back to Magnesium Binding Sites List in 2w02
Magnesium binding site 1 out of 2 in the Co-Complex Structure of Achromobactin Synthetase Protein D (Acsd) with Atp 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 From Pectobacterium Chrysanthemi within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1589

b:22.4
occ:1.00
O3G A:ATP1588 2.2 17.6 1.0
OD1 A:ASN447 2.2 9.0 1.0
OE1 A:GLN446 2.3 12.0 1.0
OD2 A:ASP464 2.5 3.7 1.0
O1A A:ATP1588 2.5 15.6 1.0
O3A A:ATP1588 3.1 16.9 1.0
CD A:GLN446 3.3 12.8 1.0
CG A:ASN447 3.3 10.9 1.0
PA A:ATP1588 3.4 17.1 1.0
NE2 A:GLN446 3.5 8.1 1.0
CG A:ASP464 3.5 4.9 1.0
PG A:ATP1588 3.5 16.1 1.0
O1B A:ATP1588 3.8 17.7 1.0
CB A:ASP464 3.9 3.5 1.0
ND2 A:ASN447 3.9 8.4 1.0
O2G A:ATP1588 3.9 16.0 1.0
PB A:ATP1588 3.9 14.6 1.0
C5' A:ATP1588 4.0 15.7 1.0
O3B A:ATP1588 4.1 15.5 1.0
CE1 A:HIS444 4.2 14.9 1.0
O5' A:ATP1588 4.2 15.4 1.0
NE2 A:HIS444 4.3 14.8 1.0
CB A:ASN447 4.6 11.8 1.0
OD1 A:ASP464 4.6 6.0 1.0
CA A:ASN447 4.6 10.5 1.0
O2A A:ATP1588 4.6 18.0 1.0
O A:GLN446 4.6 11.8 1.0
CG A:GLN446 4.7 11.2 1.0
O1G A:ATP1588 4.7 14.5 1.0
N A:ASN447 4.7 11.4 1.0
C A:GLN446 4.7 11.3 1.0

Magnesium binding site 2 out of 2 in 2w02

Go back to Magnesium Binding Sites List in 2w02
Magnesium binding site 2 out of 2 in the Co-Complex Structure of Achromobactin Synthetase Protein D (Acsd) with Atp 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 From Pectobacterium Chrysanthemi within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg1589

b:23.4
occ:1.00
O3G B:ATP1588 2.0 9.7 1.0
OE1 B:GLN446 2.2 10.3 1.0
OD1 B:ASN447 2.3 8.8 1.0
O1A B:ATP1588 2.4 7.4 1.0
O3A B:ATP1588 2.5 7.1 1.0
OD2 B:ASP464 2.5 4.4 1.0
PA B:ATP1588 3.0 7.5 1.0
CD B:GLN446 3.2 14.0 1.0
PG B:ATP1588 3.3 10.1 1.0
CG B:ASP464 3.3 4.1 1.0
CG B:ASN447 3.5 11.5 1.0
PB B:ATP1588 3.6 6.4 1.0
NE2 B:GLN446 3.6 9.0 1.0
O3B B:ATP1588 3.6 6.0 1.0
CB B:ASP464 3.7 4.9 1.0
O1B B:ATP1588 3.8 9.0 1.0
CE1 B:HIS444 3.9 15.9 1.0
O2G B:ATP1588 3.9 5.5 1.0
C5' B:ATP1588 4.0 10.3 1.0
O5' B:ATP1588 4.0 10.4 1.0
ND2 B:ASN447 4.1 7.7 1.0
O2A B:ATP1588 4.2 7.9 1.0
OD1 B:ASP464 4.3 7.5 1.0
NE2 B:HIS444 4.3 13.5 1.0
O1G B:ATP1588 4.5 5.3 1.0
CG B:GLN446 4.6 11.9 1.0
O B:GLN446 4.6 13.2 1.0
CB B:ASN447 4.7 11.5 1.0
CA B:ASN447 4.7 11.2 1.0
C B:GLN446 4.7 12.4 1.0
N B:ASN447 4.8 11.9 1.0
C4' B:ATP1588 4.9 9.5 1.0
O2B B:ATP1588 4.9 5.3 1.0
O B:HOH2137 4.9 22.5 1.0
CB B:GLN446 5.0 12.0 1.0

Reference:

S.Schmelz, N.Kadi, S.A.Mcmahon, L.Song, D.Oves-Costales, M.Oke, H.Liu, K.A.Johnson, L.G.Carter, C.H.Botting, M.F.White, G.L.Challis, J.H.Naismith. Acsd Catalyzes Enantioselective Citrate Desymmetrization in Siderophore Biosynthesis. Nat. Chem. Biol. V. 5 174 2009.
ISSN: ESSN 1552-4469
PubMed: 19182782
DOI: 10.1038/NCHEMBIO.145
Page generated: Mon Dec 14 07:43:24 2020

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