Atomistry » Iron » PDB 3etr-3fou » 3fm4
Atomistry »
  Iron »
    PDB 3etr-3fou »
      3fm4 »

Iron in PDB 3fm4: Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii

Enzymatic activity of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii

All present enzymatic activity of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii:
1.11.1.16;

Protein crystallography data

The structure of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii, PDB code: 3fm4 was solved by K.Piontek, A.T.Martinez, T.Choinowski, D.A.Plattner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.88 / 2.11
Space group P 43
Cell size a, b, c (Å), α, β, γ (°) 62.794, 62.794, 97.875, 90.00, 90.00, 90.00
R / Rfree (%) 14.1 / 19.8

Other elements in 3fm4:

The structure of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii also contains other interesting chemical elements:

Arsenic (As) 2 atoms
Calcium (Ca) 2 atoms
Zinc (Zn) 6 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii (pdb code 3fm4). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii, PDB code: 3fm4:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in 3fm4

Go back to Iron Binding Sites List in 3fm4
Iron binding site 1 out of 3 in the Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe350

b:19.3
occ:1.00
FE A:HEM350 0.0 19.3 1.0
NA A:HEM350 2.1 17.9 1.0
NC A:HEM350 2.1 20.5 1.0
NE2 A:HIS169 2.1 18.3 1.0
ND A:HEM350 2.1 21.5 1.0
NB A:HEM350 2.1 17.2 1.0
O A:HOH510 2.9 54.7 1.0
CE1 A:HIS169 3.0 15.9 1.0
C1D A:HEM350 3.1 21.5 1.0
C1A A:HEM350 3.1 19.6 1.0
C4C A:HEM350 3.1 18.3 1.0
C4D A:HEM350 3.1 22.2 1.0
C1C A:HEM350 3.1 18.7 1.0
C4B A:HEM350 3.1 18.8 1.0
C4A A:HEM350 3.1 18.9 1.0
C1B A:HEM350 3.2 16.4 1.0
CD2 A:HIS169 3.2 16.8 1.0
CHD A:HEM350 3.4 20.1 1.0
CHA A:HEM350 3.4 17.2 1.0
CHC A:HEM350 3.5 18.4 1.0
CHB A:HEM350 3.5 17.9 1.0
ND1 A:HIS169 4.2 14.3 1.0
C2D A:HEM350 4.3 19.2 1.0
CG A:HIS169 4.3 14.7 1.0
C2A A:HEM350 4.3 17.5 1.0
C3D A:HEM350 4.3 20.1 1.0
C3C A:HEM350 4.3 19.6 1.0
C3A A:HEM350 4.3 19.2 1.0
C2C A:HEM350 4.3 18.4 1.0
C3B A:HEM350 4.3 21.6 1.0
C2B A:HEM350 4.4 19.4 1.0
O A:HOH491 4.4 41.0 1.0
CD2 A:LEU166 4.8 17.9 1.0

Iron binding site 2 out of 3 in 3fm4

Go back to Iron Binding Sites List in 3fm4
Iron binding site 2 out of 3 in the Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe335

b:14.2
occ:0.30
NE2 A:HIS293 2.0 33.4 1.0
OD2 A:ASP318 2.0 43.3 1.0
O A:HOH647 2.2 53.0 1.0
CE1 A:HIS293 2.9 40.9 1.0
CG A:ASP318 2.9 51.8 1.0
CD2 A:HIS293 3.0 40.3 1.0
OD1 A:ASP318 3.2 54.1 1.0
O A:HOH379 4.0 33.9 1.0
ND1 A:HIS293 4.0 40.0 1.0
CG A:HIS293 4.1 39.6 1.0
CB A:ASP318 4.3 53.2 1.0
O A:HOH619 4.8 60.1 1.0

Iron binding site 3 out of 3 in 3fm4

Go back to Iron Binding Sites List in 3fm4
Iron binding site 3 out of 3 in the Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure Analysis of Fungal Versatile Peroxidase From Pleurotus Eryngii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe339

b:33.0
occ:0.33
OD1 A:ASP69 2.1 33.6 1.0
O A:HOH447 2.3 45.1 1.0
O A:HOH366 2.4 22.4 0.3
O A:HOH583 2.6 37.0 1.0
CG A:ASP69 3.1 31.1 1.0
NZ A:LYS89 3.3 50.9 1.0
OD2 A:ASP69 3.5 35.4 1.0
O A:HOH368 3.9 57.9 1.0
OG1 A:THR70 4.0 38.6 1.0
O A:ALA67 4.3 24.1 1.0
O A:ILE66 4.4 20.9 1.0
N A:ASP69 4.4 25.1 1.0
CB A:ASP69 4.5 28.3 1.0
N A:THR70 4.5 27.2 1.0
CE A:LYS89 4.6 46.7 1.0
CA A:ASP69 4.9 26.3 1.0
C A:ALA67 4.9 25.3 1.0

Reference:

K.Piontek, T.Choinowski, M.Perez-Boada, F.J.Ruiz-Duenas, M.J.Martinez, D.A.Plattner, A.T.Martinez. Structural and Site-Directed Mutagenesis Study of Versatile Peroxidase Oxidizing Both Mn(II) and Aromatic Substrates To Be Published.
Page generated: Sun Dec 13 15:05:43 2020

Last articles

Zn in 7L0B
Zn in 7KZZ
Zn in 7KZL
Zn in 7L3O
Zn in 7L52
Zn in 7L6T
Zn in 7KZ7
Zn in 7L6R
Zn in 7KKM
Zn in 7KKQ
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy