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Iron in PDB 5lth: Crystal Structure of the Alpha Subunit of Heme Dependent Oxidative N- Demethylase (Hodm) in Complex with the Dimethylamine Substrate

Protein crystallography data

The structure of Crystal Structure of the Alpha Subunit of Heme Dependent Oxidative N- Demethylase (Hodm) in Complex with the Dimethylamine Substrate, PDB code: 5lth was solved by M.Ortmayer, D.Leys, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.01 / 1.76
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 80.380, 80.380, 144.790, 90.00, 90.00, 90.00
R / Rfree (%) 16.5 / 18.9

Other elements in 5lth:

The structure of Crystal Structure of the Alpha Subunit of Heme Dependent Oxidative N- Demethylase (Hodm) in Complex with the Dimethylamine Substrate also contains other interesting chemical elements:

Sodium (Na) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Alpha Subunit of Heme Dependent Oxidative N- Demethylase (Hodm) in Complex with the Dimethylamine Substrate (pdb code 5lth). 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 Structure of the Alpha Subunit of Heme Dependent Oxidative N- Demethylase (Hodm) in Complex with the Dimethylamine Substrate, PDB code: 5lth:

Iron binding site 1 out of 1 in 5lth

Go back to Iron Binding Sites List in 5lth
Iron binding site 1 out of 1 in the Crystal Structure of the Alpha Subunit of Heme Dependent Oxidative N- Demethylase (Hodm) in Complex with the Dimethylamine Substrate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of the Alpha Subunit of Heme Dependent Oxidative N- Demethylase (Hodm) in Complex with the Dimethylamine Substrate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:14.3
occ:1.00
FE A:HEM401 0.0 14.3 1.0
ND A:HEM401 2.0 13.7 1.0
NA A:HEM401 2.0 13.7 1.0
NC A:HEM401 2.1 14.9 1.0
NB A:HEM401 2.1 12.6 1.0
NE2 A:HIS194 2.2 15.5 1.0
O A:HOH705 2.5 11.6 0.5
C1D A:HEM401 3.0 15.3 1.0
C4D A:HEM401 3.0 13.8 1.0
C4A A:HEM401 3.0 14.6 1.0
C4B A:HEM401 3.0 13.6 1.0
C1B A:HEM401 3.0 14.6 1.0
C4C A:HEM401 3.1 14.7 1.0
C1A A:HEM401 3.1 13.6 1.0
CD2 A:HIS194 3.1 12.8 1.0
C1C A:HEM401 3.2 13.8 1.0
CE1 A:HIS194 3.2 15.1 1.0
CHB A:HEM401 3.4 15.4 1.0
CHD A:HEM401 3.4 15.8 1.0
CHA A:HEM401 3.5 15.2 1.0
CHC A:HEM401 3.5 12.9 1.0
O A:HOH705 3.5 11.2 0.5
C3A A:HEM401 4.2 13.5 1.0
C2D A:HEM401 4.2 15.6 1.0
C2B A:HEM401 4.3 14.2 1.0
ND1 A:HIS194 4.3 15.4 1.0
C3B A:HEM401 4.3 13.1 1.0
C3D A:HEM401 4.3 13.4 1.0
CG A:HIS194 4.3 16.2 1.0
C2A A:HEM401 4.3 14.9 1.0
C3C A:HEM401 4.3 16.9 1.0
C2C A:HEM401 4.4 16.6 1.0
NE1 A:TRP193 4.7 15.7 1.0
CE1 A:PHE206 4.7 15.9 1.0
NH1 A:ARG224 4.8 16.9 1.0
C2 A:DMN402 4.8 17.1 1.0
N1 A:DMN402 4.9 17.3 1.0

Reference:

M.Ortmayer, P.Lafite, B.R.Menon, T.Tralau, K.Fisher, L.Denkhaus, N.S.Scrutton, S.E.Rigby, A.W.Munro, S.Hay, D.Leys. An Oxidative N-Demethylase Reveals Pas Transition From Ubiquitous Sensor to Enzyme. Nature V. 539 593 2016.
ISSN: ESSN 1476-4687
PubMed: 27851736
DOI: 10.1038/NATURE20159
Page generated: Sun Dec 13 16:07:33 2020

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