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Iron in PDB 3rn0: Crystal Structure of the W199K-Maug/Pre-Methylamine Dehydrogenase Complex

Enzymatic activity of Crystal Structure of the W199K-Maug/Pre-Methylamine Dehydrogenase Complex

All present enzymatic activity of Crystal Structure of the W199K-Maug/Pre-Methylamine Dehydrogenase Complex:
1.4.99.3;

Protein crystallography data

The structure of Crystal Structure of the W199K-Maug/Pre-Methylamine Dehydrogenase Complex, PDB code: 3rn0 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) 39.58 / 1.91
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 (%) 17.3 / 23

Other elements in 3rn0:

The structure of Crystal Structure of the W199K-Maug/Pre-Methylamine Dehydrogenase Complex also contains other interesting chemical elements:

Calcium (Ca) 2 atoms
Sodium (Na) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the W199K-Maug/Pre-Methylamine Dehydrogenase Complex (pdb code 3rn0). 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 W199K-Maug/Pre-Methylamine Dehydrogenase Complex, PDB code: 3rn0:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 3rn0

Go back to Iron Binding Sites List in 3rn0
Iron binding site 1 out of 4 in the Crystal Structure of the W199K-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 W199K-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:31.7
occ:1.00
 FE A:HEC500 0.0 31.7 1.0
NE2 A:HIS35 2.0 28.6 1.0
NC A:HEC500 2.1 33.3 1.0
ND A:HEC500 2.1 29.3 1.0
NB A:HEC500 2.1 30.6 1.0
NA A:HEC500 2.1 33.7 1.0
CD2 A:HIS35 2.9 31.6 1.0
CE1 A:HIS35 3.0 29.5 1.0
C1D A:HEC500 3.1 31.2 1.0
C4C A:HEC500 3.1 35.3 1.0
C1C A:HEC500 3.1 29.5 1.0
C4B A:HEC500 3.1 33.3 1.0
C4D A:HEC500 3.1 32.3 1.0
C1B A:HEC500 3.1 33.3 1.0
C4A A:HEC500 3.1 32.1 1.0
C1A A:HEC500 3.1 29.8 1.0
O A:HOH437 3.2 21.8 1.0
CHD A:HEC500 3.4 28.9 1.0
CHB A:HEC500 3.5 28.8 1.0
CHC A:HEC500 3.5 29.9 1.0
CHA A:HEC500 3.5 27.1 1.0
NE2 A:GLN103 4.1 30.5 1.0
ND1 A:HIS35 4.1 30.0 1.0
CG A:HIS35 4.1 27.8 1.0
CG A:PRO107 4.2 37.0 1.0
C2D A:HEC500 4.4 29.0 1.0
C2C A:HEC500 4.4 30.3 1.0
C3D A:HEC500 4.4 30.6 1.0
C3C A:HEC500 4.4 29.2 1.0
C3B A:HEC500 4.4 33.5 1.0
C2B A:HEC500 4.4 31.1 1.0
C3A A:HEC500 4.4 31.2 1.0
C2A A:HEC500 4.4 30.6 1.0
CB A:PRO107 4.8 37.2 1.0

Iron binding site 2 out of 4 in 3rn0

Go back to Iron Binding Sites List in 3rn0
Iron binding site 2 out of 4 in the Crystal Structure of the W199K-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 W199K-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe600

b:28.6
occ:1.00
 FE A:HEC600 0.0 28.6 1.0
NB A:HEC600 2.0 25.3 1.0
NE2 A:HIS205 2.0 26.4 1.0
OH A:TYR294 2.1 30.7 1.0
NC A:HEC600 2.1 25.6 1.0
ND A:HEC600 2.1 25.0 1.0
NA A:HEC600 2.1 25.1 1.0
CZ A:TYR294 2.9 31.7 1.0
C1B A:HEC600 3.0 29.6 1.0
CE1 A:HIS205 3.0 27.4 1.0
CD2 A:HIS205 3.0 28.1 1.0
C4B A:HEC600 3.0 30.7 1.0
C1A A:HEC600 3.1 24.2 1.0
C1C A:HEC600 3.1 26.9 1.0
C1D A:HEC600 3.1 28.4 1.0
C4D A:HEC600 3.1 26.8 1.0
C4C A:HEC600 3.1 29.1 1.0
C4A A:HEC600 3.1 28.3 1.0
CHB A:HEC600 3.4 28.6 1.0
CHC A:HEC600 3.4 27.5 1.0
CHA A:HEC600 3.4 18.5 1.0
CHD A:HEC600 3.4 27.3 1.0
CE1 A:TYR294 3.6 27.2 1.0
CE2 A:TYR294 3.8 25.7 1.0
ND1 A:HIS205 4.1 30.6 1.0
CG A:HIS205 4.2 29.1 1.0
C2B A:HEC600 4.3 29.2 1.0
C3B A:HEC600 4.3 28.5 1.0
C3D A:HEC600 4.4 28.4 1.0
C2A A:HEC600 4.4 28.6 1.0
C2D A:HEC600 4.4 25.7 1.0
C2C A:HEC600 4.4 28.9 1.0
C3C A:HEC600 4.4 24.5 1.0
C3A A:HEC600 4.4 28.0 1.0
CD1 A:TYR294 4.9 29.2 1.0
CD2 A:TYR294 4.9 26.6 1.0

Iron binding site 3 out of 4 in 3rn0

Go back to Iron Binding Sites List in 3rn0
Iron binding site 3 out of 4 in the Crystal Structure of the W199K-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 W199K-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe500

b:25.9
occ:1.00
 FE B:HEC500 0.0 25.9 1.0
NC B:HEC500 2.1 27.2 1.0
NE2 B:HIS35 2.1 24.0 1.0
NA B:HEC500 2.1 26.9 1.0
NB B:HEC500 2.1 26.5 1.0
ND B:HEC500 2.1 26.2 1.0
O B:HOH1182 2.4 36.5 1.0
C4C B:HEC500 3.0 24.0 1.0
CE1 B:HIS35 3.0 22.7 1.0
C1C B:HEC500 3.0 24.7 1.0
C1A B:HEC500 3.0 21.1 1.0
C4A B:HEC500 3.1 24.3 1.0
C4B B:HEC500 3.1 27.5 1.0
CD2 B:HIS35 3.1 24.8 1.0
C1D B:HEC500 3.1 23.6 1.0
C1B B:HEC500 3.1 26.4 1.0
C4D B:HEC500 3.1 20.0 1.0
CHD B:HEC500 3.4 23.5 1.0
CHC B:HEC500 3.4 19.6 1.0
CHA B:HEC500 3.4 19.1 1.0
CHB B:HEC500 3.4 22.8 1.0
O B:HOH407 4.0 35.8 1.0
NE2 B:GLN103 4.1 24.9 1.0
ND1 B:HIS35 4.2 23.0 1.0
CG B:HIS35 4.2 23.6 1.0
CG B:PRO107 4.3 27.3 1.0
C3C B:HEC500 4.3 24.6 1.0
C2C B:HEC500 4.3 21.0 1.0
C2A B:HEC500 4.4 22.9 1.0
C3A B:HEC500 4.4 22.9 1.0
C3B B:HEC500 4.4 24.4 1.0
C2D B:HEC500 4.4 25.3 1.0
C2B B:HEC500 4.4 27.0 1.0
C3D B:HEC500 4.4 24.5 1.0
CB B:PRO107 5.0 29.3 1.0

Iron binding site 4 out of 4 in 3rn0

Go back to Iron Binding Sites List in 3rn0
Iron binding site 4 out of 4 in the Crystal Structure of the W199K-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 W199K-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe600

b:20.2
occ:1.00
 FE B:HEC600 0.0 20.2 1.0
OH B:TYR294 1.9 19.0 1.0
NC B:HEC600 2.0 18.5 1.0
NB B:HEC600 2.1 17.4 1.0
NA B:HEC600 2.1 21.4 1.0
ND B:HEC600 2.1 21.0 1.0
NE2 B:HIS205 2.1 19.4 1.0
CD2 B:HIS205 2.9 21.7 1.0
CZ B:TYR294 3.0 19.1 1.0
C1D B:HEC600 3.0 17.2 1.0
C1A B:HEC600 3.0 19.6 1.0
C1C B:HEC600 3.0 15.2 1.0
C4C B:HEC600 3.0 14.8 1.0
C4B B:HEC600 3.0 16.3 1.0
C4D B:HEC600 3.1 18.5 1.0
C1B B:HEC600 3.1 16.7 1.0
C4A B:HEC600 3.1 22.2 1.0
CE1 B:HIS205 3.2 15.5 1.0
CHD B:HEC600 3.3 14.6 1.0
CHA B:HEC600 3.4 15.6 1.0
CHC B:HEC600 3.4 12.2 1.0
CHB B:HEC600 3.4 20.1 1.0
CE1 B:TYR294 3.7 24.0 1.0
CE2 B:TYR294 3.8 22.2 1.0
CG B:HIS205 4.1 23.2 1.0
ND1 B:HIS205 4.2 19.7 1.0
C2D B:HEC600 4.3 18.3 1.0
C2C B:HEC600 4.3 18.1 1.0
C2A B:HEC600 4.3 18.5 1.0
C3C B:HEC600 4.3 13.5 1.0
C3D B:HEC600 4.3 17.9 1.0
C3B B:HEC600 4.3 15.5 1.0
C2B B:HEC600 4.3 19.3 1.0
C3A B:HEC600 4.4 20.1 1.0
CD1 B:TYR294 4.9 19.9 1.0

Reference:

N.A.Tarboush, L.M.Jensen, E.T.Yukl, J.Geng, A.Liu, C.M.Wilmot, V.L.Davidson. Mutagenesis of TRYPTOPHAN199 Suggests That Hopping Is Required For Maug-Dependent Tryptophan Tryptophylquinone Biosynthesis. Proc.Natl.Acad.Sci.Usa V. 108 16956 2011.
ISSN: ISSN 0027-8424
PubMed: 21969534
DOI: 10.1073/PNAS.1109423108
Page generated: Tue Aug 5 06:34:51 2025

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