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Magnesium in PDB 5oxu: Direct-Evolutioned Unspecific Peroxygenase From Agrocybe Aegerita

Enzymatic activity of Direct-Evolutioned Unspecific Peroxygenase From Agrocybe Aegerita

All present enzymatic activity of Direct-Evolutioned Unspecific Peroxygenase From Agrocybe Aegerita:
1.11.2.1;

Protein crystallography data

The structure of Direct-Evolutioned Unspecific Peroxygenase From Agrocybe Aegerita, PDB code: 5oxu was solved by M.Ramirez-Escudero, J.Sanz-Aparicio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.19 / 1.47
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 51.072, 57.939, 61.099, 90.00, 109.36, 90.00
R / Rfree (%) 16.4 / 17.8

Other elements in 5oxu:

The structure of Direct-Evolutioned Unspecific Peroxygenase From Agrocybe Aegerita also contains other interesting chemical elements:

Iron (Fe) 1 atom
Chlorine (Cl) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Direct-Evolutioned Unspecific Peroxygenase From Agrocybe Aegerita (pdb code 5oxu). 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 Direct-Evolutioned Unspecific Peroxygenase From Agrocybe Aegerita, PDB code: 5oxu:

Magnesium binding site 1 out of 1 in 5oxu

Go back to Magnesium Binding Sites List in 5oxu
Magnesium binding site 1 out of 1 in the Direct-Evolutioned Unspecific Peroxygenase From Agrocybe Aegerita


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Direct-Evolutioned Unspecific Peroxygenase From Agrocybe Aegerita within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:4.3
occ:1.00
 O A:HOH671 2.0 6.6 1.0
OE2 A:GLU122 2.1 6.4 1.0
O A:HOH585 2.1 5.0 1.0
O A:GLY123 2.1 5.6 1.0
OG A:SER126 2.1 5.7 1.0
O1A A:HEM401 2.2 6.9 1.0
CD A:GLU122 3.1 6.7 1.0
CGA A:HEM401 3.1 7.0 1.0
C A:GLY123 3.2 5.8 1.0
CB A:SER126 3.3 5.8 1.0
O2A A:HEM401 3.4 7.3 1.0
CG A:GLU122 3.6 6.9 1.0
N A:GLY123 3.6 6.3 1.0
CA A:GLY123 3.9 6.0 1.0
O A:HOH659 4.0 6.5 1.0
O A:HOH638 4.2 6.5 1.0
OE1 A:GLU122 4.2 6.6 1.0
O A:HOH523 4.2 5.4 1.0
O A:ASN137 4.2 7.2 1.0
N A:ASP124 4.3 5.6 1.0
CA A:SER126 4.4 5.9 1.0
N A:SER126 4.4 5.8 1.0
NH2 A:ARG189 4.4 7.0 1.0
CBA A:HEM401 4.5 6.8 1.0
CA A:ASP124 4.6 5.7 1.0
C A:GLU122 4.6 6.8 1.0
O A:GLY130 4.7 5.7 1.0
CZ A:ARG189 4.8 7.1 1.0
CB A:GLU122 4.8 7.0 1.0
CB A:ARG129 4.8 6.1 1.0
C A:ASP124 4.8 5.7 1.0
CAA A:HEM401 4.9 6.7 1.0
CA A:GLU122 4.9 7.2 1.0
CB A:ASN137 5.0 7.3 1.0
O A:ASP124 5.0 5.7 1.0

Reference:

M.Ramirez-Escudero, P.Molina-Espeja, P.Gomez De Santos, M.Hofrichter, J.Sanz-Aparicio, M.Alcalde. Structural Insights Into the Substrate Promiscuity of A Laboratory-Evolved Peroxygenase. Acs Chem.Biol. V. 13 3259 2018.
ISSN: ESSN 1554-8937
PubMed: 30376293
DOI: 10.1021/ACSCHEMBIO.8B00500
Page generated: Tue Aug 12 17:51:34 2025

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