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Iron in PDB 3rmz: Crystal Structure of the W199F-Maug/Pre-Methylamine Dehydrogenase Complex

Enzymatic activity of Crystal Structure of the W199F-Maug/Pre-Methylamine Dehydrogenase Complex

All present enzymatic activity of Crystal Structure of the W199F-Maug/Pre-Methylamine Dehydrogenase Complex:
1.4.99.3;

Protein crystallography data

The structure of Crystal Structure of the W199F-Maug/Pre-Methylamine Dehydrogenase Complex, PDB code: 3rmz 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 / 1.72
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 (%) 13.8 / 18.1

Other elements in 3rmz:

The structure of Crystal Structure of the W199F-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 W199F-Maug/Pre-Methylamine Dehydrogenase Complex (pdb code 3rmz). 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 W199F-Maug/Pre-Methylamine Dehydrogenase Complex, PDB code: 3rmz:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 3rmz

Go back to Iron Binding Sites List in 3rmz
Iron binding site 1 out of 4 in the Crystal Structure of the W199F-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 W199F-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:15.1
occ:1.00
 FE A:HEC500 0.0 15.1 1.0
NB A:HEC500 2.0 13.3 1.0
NC A:HEC500 2.0 15.9 1.0
ND A:HEC500 2.0 15.0 1.0
NA A:HEC500 2.1 15.8 1.0
NE2 A:HIS35 2.1 17.1 1.0
O A:HOH1962 2.5 18.9 0.5
C4D A:HEC500 3.0 12.8 1.0
C4B A:HEC500 3.0 15.2 1.0
C1D A:HEC500 3.0 16.1 1.0
C1A A:HEC500 3.0 15.8 1.0
C1C A:HEC500 3.0 14.2 1.0
C1B A:HEC500 3.0 16.0 1.0
C4A A:HEC500 3.0 13.4 1.0
C4C A:HEC500 3.1 15.3 1.0
CD2 A:HIS35 3.1 14.9 1.0
CE1 A:HIS35 3.1 11.6 1.0
CHD A:HEC500 3.4 14.2 1.0
CHA A:HEC500 3.4 13.3 1.0
CHC A:HEC500 3.5 13.2 1.0
CHB A:HEC500 3.5 13.9 1.0
O A:HOH438 3.8 13.2 0.5
NE2 A:GLN103 4.1 17.6 1.0
ND1 A:HIS35 4.3 13.0 1.0
CG A:HIS35 4.3 13.1 1.0
CG A:PRO107 4.3 20.8 1.0
C2C A:HEC500 4.3 14.5 1.0
C2D A:HEC500 4.3 14.8 1.0
C3C A:HEC500 4.3 14.5 1.0
C2A A:HEC500 4.3 13.1 1.0
C2B A:HEC500 4.3 15.4 1.0
C3D A:HEC500 4.3 15.8 1.0
C3A A:HEC500 4.3 13.7 1.0
C3B A:HEC500 4.3 14.2 1.0
CB A:PRO107 4.9 19.6 1.0
CD2 A:LEU70 5.0 16.4 1.0

Iron binding site 2 out of 4 in 3rmz

Go back to Iron Binding Sites List in 3rmz
Iron binding site 2 out of 4 in the Crystal Structure of the W199F-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 W199F-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe600

b:13.9
occ:1.00
 FE A:HEC600 0.0 13.9 1.0
OH A:TYR294 1.9 14.6 1.0
NB A:HEC600 2.0 12.7 1.0
NA A:HEC600 2.0 11.3 1.0
ND A:HEC600 2.0 11.1 1.0
NC A:HEC600 2.0 12.2 1.0
NE2 A:HIS205 2.1 12.1 1.0
CZ A:TYR294 2.9 16.1 1.0
C4C A:HEC600 3.0 10.7 1.0
C1B A:HEC600 3.0 11.3 1.0
C1A A:HEC600 3.0 13.3 1.0
C4B A:HEC600 3.0 14.3 1.0
CD2 A:HIS205 3.0 12.9 1.0
C1C A:HEC600 3.0 13.7 1.0
C4D A:HEC600 3.0 11.9 1.0
C4A A:HEC600 3.0 11.8 1.0
C1D A:HEC600 3.0 12.9 1.0
CE1 A:HIS205 3.1 12.7 1.0
CHB A:HEC600 3.4 12.5 1.0
CHA A:HEC600 3.4 9.8 1.0
CHD A:HEC600 3.4 11.8 1.0
CHC A:HEC600 3.4 12.1 1.0
CE1 A:TYR294 3.6 15.5 1.0
CE2 A:TYR294 3.8 14.0 1.0
ND1 A:HIS205 4.2 12.0 1.0
CG A:HIS205 4.2 14.1 1.0
C2B A:HEC600 4.3 13.2 1.0
C3C A:HEC600 4.3 11.7 1.0
C2C A:HEC600 4.3 14.3 1.0
C3B A:HEC600 4.3 14.9 1.0
C3D A:HEC600 4.3 10.4 1.0
C2A A:HEC600 4.3 15.8 1.0
C3A A:HEC600 4.3 10.3 1.0
C2D A:HEC600 4.3 11.6 1.0
CD1 A:TYR294 4.9 13.4 1.0
CD2 A:TYR294 5.0 14.5 1.0

Iron binding site 3 out of 4 in 3rmz

Go back to Iron Binding Sites List in 3rmz
Iron binding site 3 out of 4 in the Crystal Structure of the W199F-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 W199F-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe500

b:15.3
occ:1.00
 FE B:HEC500 0.0 15.3 1.0
NA B:HEC500 2.0 14.1 1.0
ND B:HEC500 2.0 14.2 1.0
NB B:HEC500 2.0 14.6 1.0
NC B:HEC500 2.1 17.9 1.0
NE2 B:HIS35 2.1 14.5 1.0
O B:HOH1931 2.2 17.0 0.5
C4A B:HEC500 3.0 12.3 1.0
C4D B:HEC500 3.0 15.0 1.0
C1B B:HEC500 3.0 14.1 1.0
C4B B:HEC500 3.0 14.3 1.0
C4C B:HEC500 3.0 13.8 1.0
C1A B:HEC500 3.1 15.3 1.0
C1D B:HEC500 3.1 14.9 1.0
C1C B:HEC500 3.1 16.3 1.0
CE1 B:HIS35 3.1 11.2 1.0
CD2 B:HIS35 3.1 16.6 1.0
CHD B:HEC500 3.4 12.9 1.0
CHA B:HEC500 3.4 14.3 1.0
CHB B:HEC500 3.4 13.1 1.0
CHC B:HEC500 3.4 14.0 1.0
O B:HOH407 3.8 16.1 0.5
NE2 B:GLN103 4.2 15.0 1.0
ND1 B:HIS35 4.2 14.7 1.0
CG B:HIS35 4.3 14.8 1.0
C2B B:HEC500 4.3 14.3 1.0
CG B:PRO107 4.3 23.1 1.0
C3B B:HEC500 4.3 14.0 1.0
C3A B:HEC500 4.3 12.9 1.0
C2D B:HEC500 4.3 14.7 1.0
C2A B:HEC500 4.3 11.8 1.0
C3C B:HEC500 4.3 14.1 1.0
C3D B:HEC500 4.4 14.5 1.0
C2C B:HEC500 4.4 16.0 1.0
CB B:PRO107 4.9 22.2 1.0
CD2 B:LEU70 5.0 17.5 1.0

Iron binding site 4 out of 4 in 3rmz

Go back to Iron Binding Sites List in 3rmz
Iron binding site 4 out of 4 in the Crystal Structure of the W199F-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 W199F-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe600

b:12.0
occ:1.00
 FE B:HEC600 0.0 12.0 1.0
OH B:TYR294 1.9 9.7 1.0
ND B:HEC600 2.0 9.4 1.0
NE2 B:HIS205 2.0 8.4 1.0
NA B:HEC600 2.0 11.6 1.0
NB B:HEC600 2.0 13.3 1.0
NC B:HEC600 2.0 10.3 1.0
CZ B:TYR294 2.9 12.5 1.0
CD2 B:HIS205 2.9 9.8 1.0
C1D B:HEC600 3.0 11.9 1.0
C1A B:HEC600 3.0 10.5 1.0
C4D B:HEC600 3.0 8.6 1.0
CE1 B:HIS205 3.0 12.0 1.0
C4B B:HEC600 3.0 9.7 1.0
C1C B:HEC600 3.0 8.4 1.0
C4C B:HEC600 3.0 7.8 1.0
C4A B:HEC600 3.0 10.9 1.0
C1B B:HEC600 3.1 11.5 1.0
CHD B:HEC600 3.4 9.1 1.0
CHA B:HEC600 3.4 8.5 1.0
CHC B:HEC600 3.4 10.9 1.0
CHB B:HEC600 3.5 12.0 1.0
CE1 B:TYR294 3.6 11.3 1.0
CE2 B:TYR294 3.7 12.8 1.0
CG B:HIS205 4.1 9.5 1.0
ND1 B:HIS205 4.1 11.0 1.0
C3D B:HEC600 4.3 11.9 1.0
C2D B:HEC600 4.3 10.1 1.0
C3A B:HEC600 4.3 9.9 1.0
C3C B:HEC600 4.3 9.1 1.0
C2A B:HEC600 4.3 12.3 1.0
C3B B:HEC600 4.3 13.5 1.0
C2C B:HEC600 4.3 11.0 1.0
C2B B:HEC600 4.3 12.5 1.0
CD1 B:TYR294 4.9 10.9 1.0
CD2 B:TYR294 4.9 11.5 1.0
CD1 B:ILE226 5.0 10.0 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: Sun Aug 4 19:41:46 2024

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