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Iron in PDB 1llp: Lignin Peroxidase (Isozyme H2) Pi 4.15

Protein crystallography data

The structure of Lignin Peroxidase (Isozyme H2) Pi 4.15, PDB code: 1llp was solved by T.H.Choinowski, K.Piontek, T.Glumoff, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 60.700, 74.710, 106.350, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Other elements in 1llp:

The structure of Lignin Peroxidase (Isozyme H2) Pi 4.15 also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Lignin Peroxidase (Isozyme H2) Pi 4.15 (pdb code 1llp). 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 Lignin Peroxidase (Isozyme H2) Pi 4.15, PDB code: 1llp:

Iron binding site 1 out of 1 in 1llp

Go back to Iron Binding Sites List in 1llp
Iron binding site 1 out of 1 in the Lignin Peroxidase (Isozyme H2) Pi 4.15


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Lignin Peroxidase (Isozyme H2) Pi 4.15 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe350

b:6.6
occ:1.00
FE A:HEM350 0.0 6.6 1.0
ND A:HEM350 2.0 5.2 1.0
NB A:HEM350 2.0 6.5 1.0
NC A:HEM350 2.1 6.0 1.0
NA A:HEM350 2.1 5.8 1.0
NE2 A:HIS176 2.2 4.7 1.0
O A:HOH399 2.3 8.5 1.0
O A:HOH398 2.9 55.1 1.0
C4D A:HEM350 3.0 5.5 1.0
C4B A:HEM350 3.0 6.7 1.0
C1C A:HEM350 3.1 6.2 1.0
C1D A:HEM350 3.1 5.1 1.0
C1A A:HEM350 3.1 5.9 1.0
C1B A:HEM350 3.1 6.2 1.0
CE1 A:HIS176 3.1 5.7 1.0
C4A A:HEM350 3.1 5.8 1.0
CD2 A:HIS176 3.2 5.2 1.0
C4C A:HEM350 3.2 5.9 1.0
CHC A:HEM350 3.4 6.5 1.0
CHA A:HEM350 3.4 5.5 1.0
CHB A:HEM350 3.4 5.8 1.0
CHD A:HEM350 3.5 5.1 1.0
C3D A:HEM350 4.2 5.5 1.0
ND1 A:HIS176 4.3 5.7 1.0
CG A:HIS176 4.3 5.4 1.0
C2D A:HEM350 4.3 5.3 1.0
C3B A:HEM350 4.3 7.1 1.0
C2A A:HEM350 4.3 6.0 1.0
C2B A:HEM350 4.3 6.6 1.0
C2C A:HEM350 4.3 6.3 1.0
C3A A:HEM350 4.3 6.1 1.0
C3C A:HEM350 4.4 6.2 1.0
O A:HOH680 4.5 11.2 1.0
O A:HOH681 4.6 23.8 1.0

Reference:

T.Choinowski, W.Blodig, K.H.Winterhalter, K.Piontek. The Crystal Structure of Lignin Peroxidase at 1.70 A Resolution Reveals A Hydroxy Group on the Cbeta of Tryptophan 171: A Novel Radical Site Formed During the Redox Cycle. J.Mol.Biol. V. 286 809 1999.
ISSN: ISSN 0022-2836
PubMed: 10024453
DOI: 10.1006/JMBI.1998.2507
Page generated: Sun Dec 13 14:22:13 2020

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