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Iron in PDB 6el0: Direct-Evolutioned Unspecific Peroxygenase From Agrocybe Aegerita, in Complex with Styrene

Enzymatic activity of Direct-Evolutioned Unspecific Peroxygenase From Agrocybe Aegerita, in Complex with Styrene

All present enzymatic activity of Direct-Evolutioned Unspecific Peroxygenase From Agrocybe Aegerita, in Complex with Styrene:
1.11.2.1;

Protein crystallography data

The structure of Direct-Evolutioned Unspecific Peroxygenase From Agrocybe Aegerita, in Complex with Styrene, PDB code: 6el0 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) 45.19 / 1.65
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 51.229, 57.731, 61.018, 90.00, 109.70, 90.00
R / Rfree (%) 15.4 / 17.4

Other elements in 6el0:

The structure of Direct-Evolutioned Unspecific Peroxygenase From Agrocybe Aegerita, in Complex with Styrene also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Chlorine (Cl) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Direct-Evolutioned Unspecific Peroxygenase From Agrocybe Aegerita, in Complex with Styrene (pdb code 6el0). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Direct-Evolutioned Unspecific Peroxygenase From Agrocybe Aegerita, in Complex with Styrene, PDB code: 6el0:

Iron binding site 1 out of 1 in 6el0

Go back to Iron Binding Sites List in 6el0
Iron binding site 1 out of 1 in the Direct-Evolutioned Unspecific Peroxygenase From Agrocybe Aegerita, in Complex with Styrene


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Direct-Evolutioned Unspecific Peroxygenase From Agrocybe Aegerita, in Complex with Styrene within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:10.8
occ:1.00
 FE A:HEM401 0.0 10.8 1.0
ND A:HEM401 1.9 10.5 1.0
NA A:HEM401 2.0 10.9 1.0
NC A:HEM401 2.1 11.3 1.0
NB A:HEM401 2.1 11.4 1.0
CAA A:SYN413 2.2 28.1 0.8
SG A:CYS36 2.5 8.7 1.0
CAB A:SYN413 2.7 29.8 0.8
C4D A:HEM401 2.9 10.5 1.0
C1D A:HEM401 2.9 10.6 1.0
C1A A:HEM401 3.0 11.0 1.0
C4B A:HEM401 3.0 11.7 1.0
C4A A:HEM401 3.1 11.2 1.0
C4C A:HEM401 3.1 11.1 1.0
C1B A:HEM401 3.1 11.7 1.0
C1C A:HEM401 3.1 11.6 1.0
CHA A:HEM401 3.4 10.7 1.0
CHD A:HEM401 3.4 10.8 1.0
CHC A:HEM401 3.4 11.8 1.0
CHB A:HEM401 3.4 11.4 1.0
CB A:CYS36 3.5 8.6 1.0
CAH A:SYN413 4.0 30.7 0.8
C2D A:HEM401 4.2 10.5 1.0
C3D A:HEM401 4.2 10.7 1.0
C2A A:HEM401 4.2 11.0 1.0
C3A A:HEM401 4.2 11.0 1.0
C2C A:HEM401 4.3 11.8 1.0
C3C A:HEM401 4.3 11.7 1.0
C2B A:HEM401 4.3 11.9 1.0
C3B A:HEM401 4.3 11.8 1.0
CA A:CYS36 4.3 8.8 1.0
CAG A:SYN413 4.6 31.6 0.8
CAF A:SYN413 4.8 31.0 0.8
CD2 A:PHE199 4.9 11.5 1.0
CE2 A:PHE199 4.9 11.5 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: Wed Aug 6 05:42:06 2025

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