Magnesium in PDB 4brs: Structure of Wild Type PHAZ7 Phb Depolymerase

All present enzymatic activity of Structure of Wild Type PHAZ7 Phb Depolymerase:
3.1.1.75;

The structure of Structure of Wild Type PHAZ7 Phb Depolymerase, PDB code: 4brs was solved by S.Hermawan, B.Subedi, A.C.Papageorgiou, D.Jendrossek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	21.923 / 1.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	41.400, 199.700, 44.200, 90.00, 114.20, 90.00
R / Rfree (%)	13.17 / 17.04

The structure of Structure of Wild Type PHAZ7 Phb Depolymerase also contains other interesting chemical elements:

Chlorine	(Cl)	1 atom
Sodium	(Na)	3 atoms

The binding sites of Magnesium atom in the Structure of Wild Type PHAZ7 Phb Depolymerase (pdb code 4brs). 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 Structure of Wild Type PHAZ7 Phb Depolymerase, PDB code: 4brs:

Magnesium binding site 1 out of 1 in the Structure of Wild Type PHAZ7 Phb Depolymerase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Wild Type PHAZ7 Phb Depolymerase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1344 b:21.7 occ:1.00 O A:HOH2564 2.7 18.1 1.0 OD2 A:ASP119 2.9 9.5 1.0 OG1 A:THR116 3.0 8.3 1.0 CB A:THR116 3.7 6.6 1.0 CG2 A:THR116 3.7 6.7 1.0 CA A:THR116 3.7 3.7 1.0 CG A:ASP119 3.8 9.0 1.0 CB A:ASP119 3.8 6.4 1.0 NZ A:LYS115 4.3 10.3 1.0 N A:THR116 4.5 7.7 1.0 O A:HOH2057 4.6 19.4 1.0 O A:THR116 4.6 6.6 1.0 C A:THR116 4.7 6.4 1.0 O A:HOH2179 4.8 17.6 1.0 O A:HOH2307 4.9 8.2 1.0 O A:LYS115 4.9 8.4 1.0 OD1 A:ASP119 5.0 10.5 1.0

D.Jendrossek, S.Hermawan, B.Subedi, A.C.Papageorgiou. Biochemical Analysis and Structure Determination of Paucimonas Lemoignei Poly(3-Hydroxybutyrate) (Phb) Depolymerase PHAZ7 Muteins Reveal the Phb Binding Site and Details of Substrate-Enzyme Interactions. Mol.Microbiol. V. 90 649 2013.
ISSN: ISSN 0950-382X
PubMed: 24007310
DOI: 10.1111/MMI.12391