Iron in PDB 3l4m: Crystal Structure of the Maug/Pre-Methylamine Dehydrogenase Complex.

All present enzymatic activity of Crystal Structure of the Maug/Pre-Methylamine Dehydrogenase Complex.:
1.4.99.3;

The structure of Crystal Structure of the Maug/Pre-Methylamine Dehydrogenase Complex., PDB code: 3l4m was solved by L.M.R.Jensen, C.M.Wilmot, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.49 / 2.02
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	55.527, 83.524, 107.782, 109.94, 91.54, 105.78
R / Rfree (%)	13.5 / 18.9

The structure of Crystal Structure of the Maug/Pre-Methylamine Dehydrogenase Complex. also contains other interesting chemical elements:

Calcium

(Ca)

2 atoms

The binding sites of Iron atom in the Crystal Structure of the Maug/Pre-Methylamine Dehydrogenase Complex. (pdb code 3l4m). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of the Maug/Pre-Methylamine Dehydrogenase Complex., PDB code: 3l4m:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystal Structure of the Maug/Pre-Methylamine Dehydrogenase Complex.


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 Maug/Pre-Methylamine Dehydrogenase Complex. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:10.1 occ:1.00 FE A:HEC500 0.0 10.1 1.0 NB A:HEC500 2.1 9.2 1.0 NA A:HEC500 2.1 9.7 1.0 ND A:HEC500 2.1 13.0 1.0 NC A:HEC500 2.1 9.5 1.0 NE2 A:HIS35 2.2 13.0 1.0 C1A A:HEC500 3.1 8.9 1.0 C1C A:HEC500 3.1 9.1 1.0 C4C A:HEC500 3.1 9.7 1.0 C1B A:HEC500 3.1 8.6 1.0 C4D A:HEC500 3.1 10.7 1.0 C4A A:HEC500 3.1 10.5 1.0 C1D A:HEC500 3.1 12.1 1.0 C4B A:HEC500 3.1 8.7 1.0 CD2 A:HIS35 3.1 11.8 1.0 CE1 A:HIS35 3.1 10.3 1.0 CHA A:HEC500 3.4 8.5 1.0 CHB A:HEC500 3.4 6.7 1.0 CHD A:HEC500 3.4 11.1 1.0 CHC A:HEC500 3.5 6.1 1.0 O A:HOH436 3.7 26.8 1.0 ND1 A:HIS35 4.3 10.3 1.0 CG A:HIS35 4.3 10.1 1.0 CG A:PRO107 4.3 12.2 1.0 NE2 A:GLN103 4.4 11.6 1.0 C2A A:HEC500 4.4 8.0 1.0 C2D A:HEC500 4.4 12.2 1.0 C2B A:HEC500 4.4 8.5 1.0 C3A A:HEC500 4.4 7.4 1.0 C3D A:HEC500 4.4 12.9 1.0 C2C A:HEC500 4.4 9.0 1.0 C3C A:HEC500 4.4 9.4 1.0 C3B A:HEC500 4.4 7.5 1.0 CB A:PRO107 4.9 12.1 1.0 CD2 A:LEU70 5.0 7.9 1.0

Iron binding site 2 out of 4 in the Crystal Structure of the Maug/Pre-Methylamine Dehydrogenase Complex.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of the Maug/Pre-Methylamine Dehydrogenase Complex. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe600 b:11.1 occ:1.00 FE A:HEC600 0.0 11.1 1.0 OH A:TYR294 2.0 8.6 1.0 NC A:HEC600 2.1 12.4 1.0 NE2 A:HIS205 2.1 6.8 1.0 ND A:HEC600 2.1 10.6 1.0 NB A:HEC600 2.1 8.9 1.0 NA A:HEC600 2.1 12.2 1.0 CZ A:TYR294 3.0 9.9 1.0 CD2 A:HIS205 3.0 9.5 1.0 C1C A:HEC600 3.0 9.1 1.0 C4C A:HEC600 3.1 10.3 1.0 C4A A:HEC600 3.1 9.2 1.0 C1B A:HEC600 3.1 8.7 1.0 C1D A:HEC600 3.1 8.7 1.0 C4D A:HEC600 3.1 9.2 1.0 CE1 A:HIS205 3.1 7.3 1.0 C1A A:HEC600 3.1 8.7 1.0 C4B A:HEC600 3.1 6.4 1.0 CHB A:HEC600 3.4 9.5 1.0 CHC A:HEC600 3.4 9.1 1.0 CHD A:HEC600 3.4 4.9 1.0 CHA A:HEC600 3.5 6.4 1.0 CE1 A:TYR294 3.7 9.5 1.0 CE2 A:TYR294 3.8 7.8 1.0 CG A:HIS205 4.2 7.7 1.0 ND1 A:HIS205 4.2 7.7 1.0 C2C A:HEC600 4.3 10.1 1.0 C3C A:HEC600 4.3 10.3 1.0 C2D A:HEC600 4.3 7.1 1.0 C3D A:HEC600 4.4 10.3 1.0 C3A A:HEC600 4.4 9.4 1.0 C2A A:HEC600 4.4 10.3 1.0 C2B A:HEC600 4.4 9.5 1.0 C3B A:HEC600 4.4 9.2 1.0 CD1 A:TYR294 4.9 10.6 1.0 CD2 A:TYR294 5.0 8.2 1.0

Iron binding site 3 out of 4 in the Crystal Structure of the Maug/Pre-Methylamine Dehydrogenase Complex.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of the Maug/Pre-Methylamine Dehydrogenase Complex. within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe500 b:10.9 occ:1.00 FE B:HEC500 0.0 10.9 1.0 NE2 B:HIS35 2.0 10.6 1.0 NA B:HEC500 2.0 11.4 1.0 ND B:HEC500 2.1 11.2 1.0 NC B:HEC500 2.1 12.6 1.0 NB B:HEC500 2.1 11.3 1.0 CD2 B:HIS35 3.0 11.4 1.0 C4A B:HEC500 3.0 9.8 1.0 CE1 B:HIS35 3.0 14.5 1.0 C1A B:HEC500 3.0 10.1 1.0 C4C B:HEC500 3.1 12.0 1.0 C1D B:HEC500 3.1 12.8 1.0 C4D B:HEC500 3.1 12.3 1.0 C1B B:HEC500 3.1 9.9 1.0 C1C B:HEC500 3.1 12.5 1.0 C4B B:HEC500 3.1 11.9 1.0 CHD B:HEC500 3.4 8.5 1.0 CHB B:HEC500 3.4 10.3 1.0 CHA B:HEC500 3.4 8.3 1.0 CHC B:HEC500 3.5 12.0 1.0 O B:HOH406 3.8 33.9 1.0 ND1 B:HIS35 4.2 11.9 1.0 CG B:HIS35 4.2 9.5 1.0 NE2 B:GLN103 4.2 12.0 1.0 CG B:PRO107 4.3 16.9 1.0 C3A B:HEC500 4.3 7.8 1.0 C2A B:HEC500 4.3 10.0 1.0 C2D B:HEC500 4.4 14.5 1.0 C3C B:HEC500 4.4 12.3 1.0 C3D B:HEC500 4.4 13.3 1.0 C2C B:HEC500 4.4 12.5 1.0 C2B B:HEC500 4.4 8.1 1.0 C3B B:HEC500 4.4 9.3 1.0 CB B:PRO107 4.9 15.2 1.0 CD2 B:LEU70 4.9 10.0 1.0

Iron binding site 4 out of 4 in the Crystal Structure of the Maug/Pre-Methylamine Dehydrogenase Complex.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of the Maug/Pre-Methylamine Dehydrogenase Complex. within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe600 b:9.8 occ:1.00 FE B:HEC600 0.0 9.8 1.0 OH B:TYR294 2.0 10.2 1.0 ND B:HEC600 2.0 10.5 1.0 NC B:HEC600 2.0 8.6 1.0 NB B:HEC600 2.1 10.2 1.0 NE2 B:HIS205 2.1 9.4 1.0 NA B:HEC600 2.1 10.3 1.0 CZ B:TYR294 3.0 9.4 1.0 C4D B:HEC600 3.0 8.1 1.0 C1B B:HEC600 3.0 9.1 1.0 C1C B:HEC600 3.0 8.9 1.0 CD2 B:HIS205 3.0 7.5 1.0 C4B B:HEC600 3.1 9.8 1.0 C1D B:HEC600 3.1 10.2 1.0 C4A B:HEC600 3.1 9.7 1.0 C1A B:HEC600 3.1 9.7 1.0 C4C B:HEC600 3.1 8.9 1.0 CE1 B:HIS205 3.1 8.4 1.0 CHA B:HEC600 3.4 7.2 1.0 CHB B:HEC600 3.4 6.2 1.0 CHC B:HEC600 3.4 3.8 1.0 CHD B:HEC600 3.5 6.2 1.0 CE1 B:TYR294 3.7 9.7 1.0 CE2 B:TYR294 3.8 10.0 1.0 ND1 B:HIS205 4.2 5.0 1.0 CG B:HIS205 4.2 7.0 1.0 C3D B:HEC600 4.3 9.2 1.0 C2B B:HEC600 4.3 9.8 1.0 C2C B:HEC600 4.3 10.3 1.0 C2D B:HEC600 4.3 8.4 1.0 C3B B:HEC600 4.4 10.6 1.0 C3C B:HEC600 4.4 6.2 1.0 C2A B:HEC600 4.4 8.1 1.0 C3A B:HEC600 4.4 10.3 1.0 CD1 B:TYR294 4.9 7.9 1.0 CD2 B:TYR294 5.0 10.1 1.0

L.M.Jensen, R.Sanishvili, V.L.Davidson, C.M.Wilmot. In Crystallo Posttranslational Modification Within A Maug/Pre-Methylamine Dehydrogenase Complex. Science V. 327 1392 2010.
ISSN: ISSN 0036-8075
PubMed: 20223990
DOI: 10.1126/SCIENCE.1182492