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Iron in PDB 3rn1: Crystal Structure of the W199E-Maug/Pre-Methylamine Dehydrogenase Complex

Enzymatic activity of Crystal Structure of the W199E-Maug/Pre-Methylamine Dehydrogenase Complex

All present enzymatic activity of Crystal Structure of the W199E-Maug/Pre-Methylamine Dehydrogenase Complex:
1.4.99.3;

Protein crystallography data

The structure of Crystal Structure of the W199E-Maug/Pre-Methylamine Dehydrogenase Complex, PDB code: 3rn1 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) 43.46 / 1.93
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 (%) 14.4 / 19.2

Other elements in 3rn1:

The structure of Crystal Structure of the W199E-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 W199E-Maug/Pre-Methylamine Dehydrogenase Complex (pdb code 3rn1). 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 W199E-Maug/Pre-Methylamine Dehydrogenase Complex, PDB code: 3rn1:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 3rn1

Go back to Iron Binding Sites List in 3rn1
Iron binding site 1 out of 4 in the Crystal Structure of the W199E-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 W199E-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:12.6
occ:1.00
 FE A:HEC500 0.0 12.6 1.0
NC A:HEC500 2.1 14.8 1.0
ND A:HEC500 2.1 14.7 1.0
NB A:HEC500 2.1 12.6 1.0
NA A:HEC500 2.1 13.5 1.0
NE2 A:HIS35 2.2 13.7 1.0
C1C A:HEC500 3.0 13.4 1.0
C4D A:HEC500 3.1 10.4 1.0
C1A A:HEC500 3.1 11.5 1.0
C1D A:HEC500 3.1 14.8 1.0
C1B A:HEC500 3.1 13.4 1.0
C4C A:HEC500 3.1 12.5 1.0
C4B A:HEC500 3.1 12.3 1.0
C4A A:HEC500 3.1 12.3 1.0
CD2 A:HIS35 3.2 9.8 1.0
CE1 A:HIS35 3.2 6.8 1.0
CHA A:HEC500 3.4 9.5 1.0
CHB A:HEC500 3.4 10.9 1.0
CHC A:HEC500 3.4 10.8 1.0
CHD A:HEC500 3.5 13.3 1.0
O A:HOH435 3.7 28.0 1.0
NE2 A:GLN103 4.2 14.9 1.0
CG A:PRO107 4.3 12.5 1.0
ND1 A:HIS35 4.3 12.5 1.0
C2C A:HEC500 4.3 11.0 1.0
CG A:HIS35 4.3 11.3 1.0
C3C A:HEC500 4.4 9.9 1.0
C3D A:HEC500 4.4 11.4 1.0
C2D A:HEC500 4.4 12.3 1.0
C2A A:HEC500 4.4 10.9 1.0
C2B A:HEC500 4.4 13.2 1.0
C3A A:HEC500 4.4 10.1 1.0
C3B A:HEC500 4.4 10.8 1.0
CB A:PRO107 4.9 14.6 1.0

Iron binding site 2 out of 4 in 3rn1

Go back to Iron Binding Sites List in 3rn1
Iron binding site 2 out of 4 in the Crystal Structure of the W199E-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 W199E-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe600

b:11.5
occ:1.00
 FE A:HEC600 0.0 11.5 1.0
OH A:TYR294 2.0 10.9 1.0
NB A:HEC600 2.0 10.8 1.0
NC A:HEC600 2.1 9.9 1.0
NE2 A:HIS205 2.1 9.2 1.0
NA A:HEC600 2.1 12.0 1.0
ND A:HEC600 2.1 12.2 1.0
CZ A:TYR294 3.0 8.7 1.0
C4C A:HEC600 3.0 9.6 1.0
C1B A:HEC600 3.0 11.4 1.0
CD2 A:HIS205 3.0 8.9 1.0
CE1 A:HIS205 3.0 10.1 1.0
C4B A:HEC600 3.1 10.2 1.0
C1C A:HEC600 3.1 8.9 1.0
C4A A:HEC600 3.1 8.2 1.0
C1D A:HEC600 3.1 11.3 1.0
C4D A:HEC600 3.1 9.3 1.0
C1A A:HEC600 3.1 8.8 1.0
CHD A:HEC600 3.4 11.9 1.0
CHB A:HEC600 3.4 10.0 1.0
CHA A:HEC600 3.4 8.8 1.0
CHC A:HEC600 3.4 8.7 1.0
CE1 A:TYR294 3.7 8.9 1.0
CE2 A:TYR294 3.8 7.4 1.0
ND1 A:HIS205 4.2 10.3 1.0
CG A:HIS205 4.2 9.4 1.0
C3C A:HEC600 4.3 11.9 1.0
C3A A:HEC600 4.3 8.3 1.0
C2B A:HEC600 4.3 10.8 1.0
C2C A:HEC600 4.3 10.2 1.0
C3B A:HEC600 4.3 11.9 1.0
C2A A:HEC600 4.4 9.8 1.0
C3D A:HEC600 4.4 12.7 1.0
C2D A:HEC600 4.4 9.4 1.0
CD1 A:TYR294 5.0 10.6 1.0
CD2 A:TYR294 5.0 7.8 1.0

Iron binding site 3 out of 4 in 3rn1

Go back to Iron Binding Sites List in 3rn1
Iron binding site 3 out of 4 in the Crystal Structure of the W199E-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 W199E-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe500

b:12.7
occ:1.00
 FE B:HEC500 0.0 12.7 1.0
NA B:HEC500 2.0 11.7 1.0
ND B:HEC500 2.1 11.8 1.0
NC B:HEC500 2.1 13.1 1.0
NB B:HEC500 2.1 14.4 1.0
NE2 B:HIS35 2.1 10.2 1.0
CE1 B:HIS35 3.0 13.5 1.0
C1A B:HEC500 3.0 11.2 1.0
C4D B:HEC500 3.1 12.7 1.0
C4A B:HEC500 3.1 11.4 1.0
C4B B:HEC500 3.1 14.4 1.0
C1C B:HEC500 3.1 12.1 1.0
C1D B:HEC500 3.1 11.5 1.0
C4C B:HEC500 3.1 11.1 1.0
CD2 B:HIS35 3.1 10.0 1.0
C1B B:HEC500 3.1 11.2 1.0
CHA B:HEC500 3.4 8.1 1.0
CHC B:HEC500 3.4 15.5 1.0
CHD B:HEC500 3.5 13.2 1.0
CHB B:HEC500 3.5 9.3 1.0
O B:HOH408 3.5 34.9 1.0
ND1 B:HIS35 4.2 14.2 1.0
CG B:PRO107 4.2 18.2 1.0
NE2 B:GLN103 4.2 15.1 1.0
CG B:HIS35 4.2 12.5 1.0
C3A B:HEC500 4.4 9.4 1.0
C2A B:HEC500 4.4 7.6 1.0
C2D B:HEC500 4.4 16.6 1.0
C3D B:HEC500 4.4 15.7 1.0
C2C B:HEC500 4.4 11.4 1.0
C3B B:HEC500 4.4 12.1 1.0
C3C B:HEC500 4.4 12.2 1.0
C2B B:HEC500 4.4 13.2 1.0
CB B:PRO107 4.9 17.3 1.0

Iron binding site 4 out of 4 in 3rn1

Go back to Iron Binding Sites List in 3rn1
Iron binding site 4 out of 4 in the Crystal Structure of the W199E-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 W199E-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe600

b:10.4
occ:1.00
 FE B:HEC600 0.0 10.4 1.0
ND B:HEC600 2.0 10.4 1.0
NB B:HEC600 2.0 10.2 1.0
OH B:TYR294 2.0 8.8 1.0
NC B:HEC600 2.0 4.7 1.0
NA B:HEC600 2.1 7.5 1.0
NE2 B:HIS205 2.1 6.3 1.0
CZ B:TYR294 3.0 12.1 1.0
C1D B:HEC600 3.0 10.4 1.0
C4B B:HEC600 3.0 7.4 1.0
C1B B:HEC600 3.0 7.6 1.0
C4C B:HEC600 3.0 5.3 1.0
C1C B:HEC600 3.0 6.2 1.0
C4D B:HEC600 3.0 6.7 1.0
C4A B:HEC600 3.1 6.1 1.0
CD2 B:HIS205 3.1 7.8 1.0
C1A B:HEC600 3.1 6.4 1.0
CE1 B:HIS205 3.1 8.9 1.0
CHD B:HEC600 3.4 6.7 1.0
CHB B:HEC600 3.4 5.7 1.0
CHC B:HEC600 3.4 4.7 1.0
CHA B:HEC600 3.5 5.8 1.0
CE1 B:TYR294 3.7 9.6 1.0
CE2 B:TYR294 3.8 9.6 1.0
ND1 B:HIS205 4.2 8.0 1.0
CG B:HIS205 4.2 7.6 1.0
C3D B:HEC600 4.3 7.9 1.0
C3B B:HEC600 4.3 9.1 1.0
C2D B:HEC600 4.3 8.1 1.0
C3C B:HEC600 4.3 7.2 1.0
C2B B:HEC600 4.3 8.9 1.0
C2C B:HEC600 4.3 6.3 1.0
C2A B:HEC600 4.4 7.0 1.0
C3A B:HEC600 4.4 7.2 1.0
CD1 B:TYR294 4.9 8.9 1.0

Reference:

L.M.R.Jensen, C.M.Wilmot. Mutagenesis of TRYPTOPHAN199 Reveals That Electron Hopping Is Required For Maug-Dependent Tryptophan Tryptophylquinone Biosynthesis To Be Published.
Page generated: Tue Aug 5 06:34:52 2025

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