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Iron in PDB 6a6q: Crystal Strcuture of A Lignin Peroxidase Isozyme H8 Variant That Is Stable at Very Acidic pH

Enzymatic activity of Crystal Strcuture of A Lignin Peroxidase Isozyme H8 Variant That Is Stable at Very Acidic pH

All present enzymatic activity of Crystal Strcuture of A Lignin Peroxidase Isozyme H8 Variant That Is Stable at Very Acidic pH:
1.11.1.14;

Protein crystallography data

The structure of Crystal Strcuture of A Lignin Peroxidase Isozyme H8 Variant That Is Stable at Very Acidic pH, PDB code: 6a6q was solved by H.Seo, K.-J.Kim, L.T.M.Pham, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.72 / 1.67
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 41.212, 99.621, 48.322, 90.00, 113.86, 90.00
R / Rfree (%) 14.2 / 17.1

Other elements in 6a6q:

The structure of Crystal Strcuture of A Lignin Peroxidase Isozyme H8 Variant That Is Stable at Very Acidic pH also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Strcuture of A Lignin Peroxidase Isozyme H8 Variant That Is Stable at Very Acidic pH (pdb code 6a6q). 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 Crystal Strcuture of A Lignin Peroxidase Isozyme H8 Variant That Is Stable at Very Acidic pH, PDB code: 6a6q:

Iron binding site 1 out of 1 in 6a6q

Go back to Iron Binding Sites List in 6a6q
Iron binding site 1 out of 1 in the Crystal Strcuture of A Lignin Peroxidase Isozyme H8 Variant That Is Stable at Very Acidic pH


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Strcuture of A Lignin Peroxidase Isozyme H8 Variant That Is Stable at Very Acidic pH within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:13.6
occ:1.00
 FE A:HEB401 0.0 13.6 1.0
ND A:HEB401 2.1 12.4 1.0
NC A:HEB401 2.1 12.9 1.0
NA A:HEB401 2.1 13.7 1.0
NB A:HEB401 2.1 13.5 1.0
NE2 A:HIS176 2.2 13.7 1.0
O A:HOH618 2.5 31.4 1.0
C1D A:HEB401 3.0 11.9 1.0
C4D A:HEB401 3.0 12.8 1.0
C1B A:HEB401 3.0 13.9 1.0
C1C A:HEB401 3.0 14.3 1.0
C4A A:HEB401 3.0 13.7 1.0
C4C A:HEB401 3.1 13.1 1.0
C1A A:HEB401 3.1 14.2 1.0
C4B A:HEB401 3.1 13.5 1.0
CE1 A:HIS176 3.2 15.1 1.0
CD2 A:HIS176 3.2 13.0 1.0
CHA A:HEB401 3.4 13.1 1.0
CHC A:HEB401 3.4 14.4 1.0
CHD A:HEB401 3.4 12.2 1.0
CHB A:HEB401 3.4 13.9 1.0
O A:HOH703 4.3 20.5 1.0
C2D A:HEB401 4.3 13.2 1.0
C3D A:HEB401 4.3 12.4 1.0
C2B A:HEB401 4.3 15.4 1.0
C3A A:HEB401 4.3 14.6 1.0
ND1 A:HIS176 4.3 15.1 1.0
C3C A:HEB401 4.3 13.7 1.0
C2C A:HEB401 4.3 14.1 1.0
C3B A:HEB401 4.4 13.7 1.0
C2A A:HEB401 4.4 13.4 1.0
CG A:HIS176 4.4 12.3 1.0
CE2 A:PHE193 4.8 17.0 1.0

Reference:

L.T.M.Pham, H.Seo, K.J.Kim, Y.H.Kim. In Silico-Designed Lignin Peroxidase Fromphanerochaete Chrysosporiumshows Enhanced Acid Stability For Depolymerization of Lignin. Biotechnol Biofuels V. 11 325 2018.
ISSN: ESSN 1754-6834
PubMed: 30555531
DOI: 10.1186/S13068-018-1324-4
Page generated: Sun Dec 13 16:19:58 2020

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