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Magnesium in PDB 2wdy: Crystal Structure of the Streptomyces Coelicolor D111A Acps Mutant in Complex with Cofactor Coa at 1.4 A

Enzymatic activity of Crystal Structure of the Streptomyces Coelicolor D111A Acps Mutant in Complex with Cofactor Coa at 1.4 A

All present enzymatic activity of Crystal Structure of the Streptomyces Coelicolor D111A Acps Mutant in Complex with Cofactor Coa at 1.4 A:
2.7.8.7;

Protein crystallography data

The structure of Crystal Structure of the Streptomyces Coelicolor D111A Acps Mutant in Complex with Cofactor Coa at 1.4 A, PDB code: 2wdy was solved by P.Dall'aglio, C.Arthur, M.P.Crump, J.Crosby, A.T.Hadfield, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 51.50 / 1.40
Space group P 21 3
Cell size a, b, c (Å), α, β, γ (°) 72.831, 72.831, 72.831, 90.00, 90.00, 90.00
R / Rfree (%) 18.875 / 21.498

Other elements in 2wdy:

The structure of Crystal Structure of the Streptomyces Coelicolor D111A Acps Mutant in Complex with Cofactor Coa at 1.4 A also contains other interesting chemical elements:

Sodium (Na) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Streptomyces Coelicolor D111A Acps Mutant in Complex with Cofactor Coa at 1.4 A (pdb code 2wdy). 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 Structure of the Streptomyces Coelicolor D111A Acps Mutant in Complex with Cofactor Coa at 1.4 A, PDB code: 2wdy:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 2wdy

Go back to Magnesium Binding Sites List in 2wdy
Magnesium binding site 1 out of 2 in the Crystal Structure of the Streptomyces Coelicolor D111A Acps Mutant in Complex with Cofactor Coa at 1.4 A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Streptomyces Coelicolor D111A Acps Mutant in Complex with Cofactor Coa at 1.4 A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1124

b:23.1
occ:0.50
MG A:MG1126 2.0 15.4 0.5
O A:HOH2202 2.6 27.7 1.0
O5A A:COA1128 2.8 25.6 0.5
O4A A:COA1128 3.0 16.0 0.5
O2A A:COA1128 3.0 12.9 0.5
O2A A:COA1128 3.1 16.0 0.5
P1A A:COA1128 3.7 12.7 0.5
OG A:SER109 3.8 16.4 1.0
CB A:ALA111 3.8 22.4 1.0
O3A A:COA1128 3.8 14.2 0.5
P2A A:COA1128 3.9 17.1 0.5
O1A A:COA1128 3.9 13.0 0.5
P2A A:COA1128 4.0 26.0 0.5
O3A A:COA1128 4.2 21.3 0.5
O A:HIS110 4.2 24.8 1.0
P1A A:COA1128 4.2 18.9 0.5
CCP A:COA1128 4.5 37.0 0.5
O6A A:COA1128 4.6 30.6 0.5
C A:HIS110 4.6 22.1 1.0
O5A A:COA1128 4.7 21.3 0.5
O A:HOH2194 4.8 19.7 1.0
CA A:ALA111 4.9 20.5 1.0
N A:ALA111 4.9 18.2 1.0
N A:HIS110 5.0 18.0 1.0

Magnesium binding site 2 out of 2 in 2wdy

Go back to Magnesium Binding Sites List in 2wdy
Magnesium binding site 2 out of 2 in the Crystal Structure of the Streptomyces Coelicolor D111A Acps Mutant in Complex with Cofactor Coa at 1.4 A


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Streptomyces Coelicolor D111A Acps Mutant in Complex with Cofactor Coa at 1.4 A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1126

b:15.4
occ:0.50
O4A A:COA1128 1.2 16.0 0.5
MG A:MG1124 2.0 23.1 0.5
O2A A:COA1128 2.1 12.9 0.5
O5A A:COA1128 2.2 25.6 0.5
O2A A:COA1128 2.2 16.0 0.5
P2A A:COA1128 2.2 17.1 0.5
O A:HOH2202 2.5 27.7 1.0
O3A A:COA1128 2.6 14.2 0.5
P1A A:COA1128 2.8 12.7 0.5
O6A A:COA1128 3.3 18.2 0.5
P1A A:COA1128 3.3 18.9 0.5
O5A A:COA1128 3.4 21.3 0.5
P2A A:COA1128 3.4 26.0 0.5
O3A A:COA1128 3.7 21.3 0.5
O1A A:COA1128 3.7 13.0 0.5
OG A:SER109 4.0 16.4 1.0
O5B A:COA1128 4.0 17.6 0.5
O5B A:COA1128 4.0 10.6 0.5
O4A A:COA1128 4.3 30.2 0.5
CCP A:COA1128 4.5 17.7 0.5
O1A A:COA1128 4.6 17.9 0.5
O6A A:COA1128 4.6 30.6 0.5
CCP A:COA1128 4.9 37.0 0.5

Reference:

P.Dall'aglio, C.Arthur, C.Williams, K.Vasilakis, H.J.Maple, J.Crosby, M.P.Crump, A.T.Hadfield. Analysis of Streptomyces Coelicolor Phosphopantetheinyl Transferase, Acps, Reveals the Basis For Relaxed Substrate Specificity. Biochemistry V. 50 5704 2011.
ISSN: ISSN 0006-2960
PubMed: 21595442
DOI: 10.1021/BI2003668
Page generated: Wed Aug 14 06:03:57 2024

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