Magnesium in PDB 6zl7: Crystal Structure of C173S Mutation in the PMGL2 Esterase From Permafrost Metagenomic Library

Enzymatic activity of Crystal Structure of C173S Mutation in the PMGL2 Esterase From Permafrost Metagenomic Library

All present enzymatic activity of Crystal Structure of C173S Mutation in the PMGL2 Esterase From Permafrost Metagenomic Library:
3.1.1.3;

Protein crystallography data

The structure of Crystal Structure of C173S Mutation in the PMGL2 Esterase From Permafrost Metagenomic Library, PDB code: 6zl7 was solved by D.A.Goryaynova, K.M.Boyko, A.Y.Nikolaeva, D.A.Korzhenevskiy, M.V.Kryukova, L.E.Petrovskaya, K.A.Novototskaya-Vlasova, E.M.Rivkina, D.A.Dolgikh, M.P.Kirpichnikov, V.O.Popov, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 56.54 / 1.50
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 47.149, 92.530, 74.410, 90.00, 106.61, 90.00
R / Rfree (%) 16.9 / 19.6

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of C173S Mutation in the PMGL2 Esterase From Permafrost Metagenomic Library (pdb code 6zl7). 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 Crystal Structure of C173S Mutation in the PMGL2 Esterase From Permafrost Metagenomic Library, PDB code: 6zl7:

Magnesium binding site 1 out of 1 in 6zl7

Go back to Magnesium Binding Sites List in 6zl7
Magnesium binding site 1 out of 1 in the Crystal Structure of C173S Mutation in the PMGL2 Esterase From Permafrost Metagenomic Library


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 C173S Mutation in the PMGL2 Esterase From Permafrost Metagenomic Library within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:8.2
occ:1.00
 O A:HOH667 3.0 29.1 1.0
N A:LEU294 3.2 8.7 1.0
N B:LEU294 3.2 9.8 1.0
NE2 A:HIS282 3.3 8.9 1.0
NE2 B:HIS282 3.4 8.8 1.0
CA B:GLU293 3.5 9.5 1.0
CA A:GLU293 3.5 9.7 1.0
CE1 A:HIS282 3.6 9.3 1.0
CE1 B:HIS282 3.6 9.3 1.0
C B:GLU293 3.9 11.0 1.0
C A:GLU293 3.9 10.7 1.0
O B:LEU294 3.9 10.2 1.0
O A:LEU294 3.9 9.3 1.0
CG A:GLU293 4.1 14.1 1.0
CG B:GLU293 4.1 14.7 1.0
O B:SER292 4.2 10.5 1.0
O A:SER292 4.2 10.9 1.0
CA A:LEU294 4.2 8.8 1.0
CA B:LEU294 4.2 9.4 1.0
CB B:GLU293 4.3 11.1 1.0
CB A:GLU293 4.3 12.6 1.0
CB A:LEU294 4.3 8.3 1.0
CB B:LEU294 4.4 10.8 1.0
C A:LEU294 4.5 8.8 1.0
C B:LEU294 4.5 10.8 1.0
CD2 A:HIS282 4.6 9.3 1.0
N A:GLU293 4.6 9.5 1.0
CD2 B:HIS282 4.6 8.4 1.0
N B:GLU293 4.6 9.0 1.0
C A:SER292 4.8 10.4 1.0
C B:SER292 4.8 9.1 1.0
ND1 A:HIS282 4.8 9.3 1.0
ND1 B:HIS282 4.8 8.1 1.0

Reference:

D.A.Goryaynova, K.M.Boyko, A.Y.Nikolaeva, D.A.Korzhenevskiy, M.V.Kryukova, L.E.Petrovskaya, K.A.Novototskaya-Vlasova, E.M.Rivkina, D.A.Dolgikh, M.P.Kirpichnikov, V.O.Popov. Crystal Structure of C173S Mutation in the PMGL2 Esterase From Permafrost Metagenomic Library To Be Published.
Page generated: Tue Dec 15 03:00:36 2020

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