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Iron in PDB 4o1q: Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex

Enzymatic activity of Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex

All present enzymatic activity of Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex:
1.4.99.3;

Protein crystallography data

The structure of Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex, PDB code: 4o1q was solved by E.T.Yukl, C.W.Wilmot, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.49 / 2.59
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 55.530, 83.520, 107.780, 109.94, 91.54, 105.78
R / Rfree (%) 19.8 / 25.4

Other elements in 4o1q:

The structure of Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex also contains other interesting chemical elements:

Calcium (Ca) 2 atoms
Sodium (Na) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex (pdb code 4o1q). 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 Q103N-Maug/Pre-Methylamine Dehydrogenase Complex, PDB code: 4o1q:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 4o1q

Go back to Iron Binding Sites List in 4o1q
Iron binding site 1 out of 4 in the Crystal Structure of the Q103N-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 Q103N-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe402

b:49.0
occ:1.00
 FE A:HEC402 0.0 49.0 1.0
ND A:HEC402 2.1 48.9 1.0
NC A:HEC402 2.1 50.6 1.0
NB A:HEC402 2.1 49.4 1.0
NA A:HEC402 2.1 47.9 1.0
NE2 A:HIS35 2.3 49.1 1.0
C4D A:HEC402 3.1 48.3 1.0
C1C A:HEC402 3.1 51.3 1.0
C4B A:HEC402 3.1 50.2 1.0
C4A A:HEC402 3.1 47.7 1.0
CD2 A:HIS35 3.1 49.9 1.0
C1D A:HEC402 3.1 49.8 1.0
C1A A:HEC402 3.1 47.3 1.0
C4C A:HEC402 3.1 51.2 1.0
C1B A:HEC402 3.1 49.0 1.0
O A:HOH563 3.4 40.4 1.0
CE1 A:HIS35 3.4 48.8 1.0
CHC A:HEC402 3.4 51.1 1.0
CHA A:HEC402 3.4 47.5 1.0
CHB A:HEC402 3.5 48.2 1.0
CHD A:HEC402 3.5 50.8 1.0
O A:HOH535 3.5 48.3 1.0
CG A:PRO107 4.0 53.5 1.0
CG A:HIS35 4.3 50.0 1.0
C3D A:HEC402 4.4 48.5 1.0
C2C A:HEC402 4.4 52.4 1.0
C2D A:HEC402 4.4 49.6 1.0
C3A A:HEC402 4.4 47.0 1.0
C2A A:HEC402 4.4 46.7 1.0
C3C A:HEC402 4.4 52.4 1.0
ND1 A:HIS35 4.4 49.3 1.0
C3B A:HEC402 4.4 50.4 1.0
C2B A:HEC402 4.4 49.7 1.0
CB A:PRO107 4.7 54.5 1.0
CG2 A:THR67 4.8 51.0 1.0

Iron binding site 2 out of 4 in 4o1q

Go back to Iron Binding Sites List in 4o1q
Iron binding site 2 out of 4 in the Crystal Structure of the Q103N-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 Q103N-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe403

b:44.8
occ:1.00
 FE A:HEC403 0.0 44.8 1.0
OH A:TYR294 1.9 45.6 1.0
NB A:HEC403 2.1 45.4 1.0
NA A:HEC403 2.1 45.3 1.0
ND A:HEC403 2.1 44.4 1.0
NC A:HEC403 2.1 44.6 1.0
NE2 A:HIS205 2.4 45.1 1.0
CZ A:TYR294 2.8 46.2 1.0
C4B A:HEC403 3.1 45.6 1.0
C1A A:HEC403 3.1 45.4 1.0
C1B A:HEC403 3.1 46.0 1.0
C4D A:HEC403 3.1 44.6 1.0
C4C A:HEC403 3.1 44.4 1.0
C4A A:HEC403 3.1 45.9 1.0
C1C A:HEC403 3.1 44.9 1.0
C1D A:HEC403 3.1 44.1 1.0
CD2 A:HIS205 3.1 45.2 1.0
CHA A:HEC403 3.4 45.1 1.0
CHC A:HEC403 3.5 45.4 1.0
CHB A:HEC403 3.5 46.1 1.0
CHD A:HEC403 3.5 44.1 1.0
CE2 A:TYR294 3.5 46.9 1.0
CE1 A:HIS205 3.5 44.9 1.0
CE1 A:TYR294 3.7 46.2 1.0
CG A:HIS205 4.4 45.1 1.0
C3B A:HEC403 4.4 46.4 1.0
C3C A:HEC403 4.4 44.6 1.0
C2B A:HEC403 4.4 46.6 1.0
C2A A:HEC403 4.4 46.0 1.0
C3A A:HEC403 4.4 46.3 1.0
C3D A:HEC403 4.4 44.4 1.0
C2D A:HEC403 4.4 44.1 1.0
C2C A:HEC403 4.4 44.8 1.0
ND1 A:HIS205 4.5 44.9 1.0
CD2 A:TYR294 4.7 47.6 1.0
CD1 A:TYR294 4.8 46.9 1.0
CD1 A:ILE226 5.0 46.1 1.0

Iron binding site 3 out of 4 in 4o1q

Go back to Iron Binding Sites List in 4o1q
Iron binding site 3 out of 4 in the Crystal Structure of the Q103N-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 Q103N-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe402

b:41.3
occ:1.00
 FE B:HEC402 0.0 41.3 1.0
NC B:HEC402 2.1 42.7 1.0
ND B:HEC402 2.1 41.4 1.0
NA B:HEC402 2.1 40.7 1.0
NB B:HEC402 2.1 41.6 1.0
NE2 B:HIS35 2.2 40.6 1.0
CD2 B:HIS35 3.0 41.2 1.0
C4D B:HEC402 3.1 41.0 1.0
C1C B:HEC402 3.1 43.4 1.0
C4C B:HEC402 3.1 43.3 1.0
C4A B:HEC402 3.1 40.6 1.0
C4B B:HEC402 3.1 42.3 1.0
C1A B:HEC402 3.1 40.3 1.0
C1D B:HEC402 3.1 42.0 1.0
C1B B:HEC402 3.1 41.4 1.0
O B:HOH573 3.1 47.8 1.0
CE1 B:HIS35 3.3 40.1 1.0
CHD B:HEC402 3.4 43.0 1.0
CHC B:HEC402 3.4 43.2 1.0
CHA B:HEC402 3.4 40.4 1.0
CHB B:HEC402 3.5 40.9 1.0
O B:HOH597 3.9 46.9 1.0
CG B:PRO107 4.1 48.5 1.0
CG B:HIS35 4.2 41.2 1.0
ND1 B:HIS35 4.3 40.6 1.0
C2A B:HEC402 4.4 40.1 1.0
C2C B:HEC402 4.4 44.5 1.0
C3D B:HEC402 4.4 41.0 1.0
C3C B:HEC402 4.4 44.4 1.0
C2D B:HEC402 4.4 41.9 1.0
C3A B:HEC402 4.4 40.1 1.0
C3B B:HEC402 4.4 42.3 1.0
C2B B:HEC402 4.4 41.7 1.0
CB B:PRO107 4.7 49.4 1.0
CG2 B:THR67 4.8 41.4 1.0

Iron binding site 4 out of 4 in 4o1q

Go back to Iron Binding Sites List in 4o1q
Iron binding site 4 out of 4 in the Crystal Structure of the Q103N-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 Q103N-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe403

b:36.7
occ:1.00
 FE B:HEC403 0.0 36.7 1.0
OH B:TYR294 1.9 35.6 1.0
NB B:HEC403 2.1 37.4 1.0
NA B:HEC403 2.1 36.9 1.0
NC B:HEC403 2.1 37.0 1.0
ND B:HEC403 2.1 36.5 1.0
NE2 B:HIS205 2.3 36.9 1.0
CZ B:TYR294 2.8 36.2 1.0
CD2 B:HIS205 3.0 37.3 1.0
C4B B:HEC403 3.1 37.6 1.0
C4C B:HEC403 3.1 36.8 1.0
C1D B:HEC403 3.1 36.3 1.0
C1A B:HEC403 3.1 36.9 1.0
C1B B:HEC403 3.1 37.8 1.0
C4D B:HEC403 3.1 36.4 1.0
C4A B:HEC403 3.1 37.2 1.0
C1C B:HEC403 3.1 37.3 1.0
CE1 B:HIS205 3.4 36.7 1.0
CHD B:HEC403 3.4 36.6 1.0
CHC B:HEC403 3.4 37.6 1.0
CHA B:HEC403 3.4 36.6 1.0
CHB B:HEC403 3.5 37.6 1.0
CE2 B:TYR294 3.5 36.7 1.0
CE1 B:TYR294 3.6 36.5 1.0
CG B:HIS205 4.3 37.5 1.0
C3B B:HEC403 4.4 38.4 1.0
C3C B:HEC403 4.4 37.4 1.0
C3D B:HEC403 4.4 36.3 1.0
C2D B:HEC403 4.4 36.3 1.0
C2B B:HEC403 4.4 38.5 1.0
C2A B:HEC403 4.4 37.2 1.0
C3A B:HEC403 4.4 37.5 1.0
ND1 B:HIS205 4.4 37.0 1.0
C2C B:HEC403 4.4 37.6 1.0
CD2 B:TYR294 4.7 37.2 1.0
CD1 B:TYR294 4.8 36.9 1.0

Reference:

S.Shin, E.T.Yukl, E.Sehanobish, C.M.Wilmot, V.L.Davidson. Site-Directed Mutagenesis of GLN103 Reveals the Influence of This Residue on the Redox Properties and Stability of Maug. Biochemistry V. 53 1342 2014.
ISSN: ISSN 0006-2960
PubMed: 24517455
DOI: 10.1021/BI5000349
Page generated: Mon Aug 5 08:04:23 2024

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