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Magnesium in PDB 2wda: The X-Ray Structure of the Streptomyces Coelicolor A3 Chondroitin Ac Lyase in Complex with Chondroitin Sulphate

Enzymatic activity of The X-Ray Structure of the Streptomyces Coelicolor A3 Chondroitin Ac Lyase in Complex with Chondroitin Sulphate

All present enzymatic activity of The X-Ray Structure of the Streptomyces Coelicolor A3 Chondroitin Ac Lyase in Complex with Chondroitin Sulphate:
4.2.2.1;

Protein crystallography data

The structure of The X-Ray Structure of the Streptomyces Coelicolor A3 Chondroitin Ac Lyase in Complex with Chondroitin Sulphate, PDB code: 2wda was solved by Z.H.Elmabrouk, E.J.Taylor, F.Vincent, N.L.Smith, J.P.Turkenburg, G.J.Davies, G.W.Black, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.68 / 2.30
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 140.508, 140.508, 100.764, 90.00, 90.00, 90.00
R / Rfree (%) 14.9 / 19.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the The X-Ray Structure of the Streptomyces Coelicolor A3 Chondroitin Ac Lyase in Complex with Chondroitin Sulphate (pdb code 2wda). 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 The X-Ray Structure of the Streptomyces Coelicolor A3 Chondroitin Ac Lyase in Complex with Chondroitin Sulphate, PDB code: 2wda:

Magnesium binding site 1 out of 1 in 2wda

Go back to Magnesium Binding Sites List in 2wda
Magnesium binding site 1 out of 1 in the The X-Ray Structure of the Streptomyces Coelicolor A3 Chondroitin Ac Lyase in Complex with Chondroitin Sulphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The X-Ray Structure of the Streptomyces Coelicolor A3 Chondroitin Ac Lyase in Complex with Chondroitin Sulphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1783

b:32.4
occ:1.00
 OG A:SER670 2.6 17.5 1.0
O A:TRP653 2.7 19.8 1.0
O A:HOH2417 2.7 3.8 0.5
N A:SER670 2.8 16.1 1.0
CB A:SER670 3.1 16.5 1.0
CA A:TRP653 3.3 19.2 1.0
C A:TRP653 3.4 18.6 1.0
CG1 A:VAL668 3.5 15.8 1.0
CA A:SER670 3.5 17.3 1.0
N A:PRO669 3.5 16.0 1.0
CB A:TRP653 3.6 17.2 1.0
CD A:PRO669 3.6 15.9 1.0
CG A:PRO669 3.8 19.1 1.0
C A:VAL668 3.9 16.4 1.0
C A:PRO669 3.9 17.2 1.0
CA A:PRO669 4.2 17.2 1.0
CA A:VAL668 4.2 15.2 1.0
CE3 A:TRP653 4.4 17.7 1.0
CB A:PRO669 4.5 17.4 1.0
O A:VAL668 4.5 18.8 1.0
CB A:VAL668 4.5 15.5 1.0
N A:TRP653 4.6 18.7 1.0
C A:SER670 4.6 18.5 1.0
CG A:TRP653 4.6 18.7 1.0
N A:LEU654 4.7 18.4 1.0
O A:HIS652 4.7 19.8 1.0
N A:LEU671 4.8 17.4 1.0
CD2 A:TRP653 4.9 18.5 1.0

Reference:

Z.H.Elmabrouk, F.Vincent, M.Zhang, N.L.Smith, J.P.Turkenburg, S.J.Charnock, G.W.Black, E.J.Taylor. Crystal Structures of A Family 8 Polysaccharide Lyase Reveal Open and Highly Occluded Substrate- Binding Cleft Conformations. Proteins V. 79 965 2011.
ISSN: ISSN 0887-3585
PubMed: 21287626
DOI: 10.1002/PROT.22938
Page generated: Wed Aug 14 06:03:51 2024

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