Atomistry » Iron » PDB 3om3-3p4q » 3orv
Atomistry »
  Iron »
    PDB 3om3-3p4q »
      3orv »

Iron in PDB 3orv: Crystal Structure of the Y294H-Maug/Pre-Methylamine Dehydrogenase Complex

Enzymatic activity of Crystal Structure of the Y294H-Maug/Pre-Methylamine Dehydrogenase Complex

All present enzymatic activity of Crystal Structure of the Y294H-Maug/Pre-Methylamine Dehydrogenase Complex:
1.4.99.3;

Protein crystallography data

The structure of Crystal Structure of the Y294H-Maug/Pre-Methylamine Dehydrogenase Complex, PDB code: 3orv 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 / 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 (%) 13.9 / 18.7

Other elements in 3orv:

The structure of Crystal Structure of the Y294H-Maug/Pre-Methylamine Dehydrogenase Complex also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Y294H-Maug/Pre-Methylamine Dehydrogenase Complex (pdb code 3orv). 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 Y294H-Maug/Pre-Methylamine Dehydrogenase Complex, PDB code: 3orv:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 3orv

Go back to Iron Binding Sites List in 3orv
Iron binding site 1 out of 4 in the Crystal Structure of the Y294H-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 Y294H-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:21.9
occ:1.00
FE A:HEC500 0.0 21.9 1.0
NA A:HEC500 2.1 23.6 1.0
ND A:HEC500 2.1 23.2 1.0
NC A:HEC500 2.1 22.1 1.0
NB A:HEC500 2.1 25.4 1.0
NE2 A:HIS35 2.1 21.0 1.0
C1A A:HEC500 3.0 22.7 1.0
C1C A:HEC500 3.1 22.8 1.0
CD2 A:HIS35 3.1 24.9 1.0
C4D A:HEC500 3.1 22.2 1.0
C4B A:HEC500 3.1 23.2 1.0
C1D A:HEC500 3.1 21.1 1.0
C4C A:HEC500 3.1 21.9 1.0
C4A A:HEC500 3.1 25.1 1.0
C1B A:HEC500 3.1 24.1 1.0
CE1 A:HIS35 3.2 20.4 1.0
CHC A:HEC500 3.4 20.0 1.0
CHA A:HEC500 3.4 21.3 1.0
CHD A:HEC500 3.5 21.8 1.0
CHB A:HEC500 3.5 22.3 1.0
O A:HOH436 3.8 32.2 1.0
NE2 A:GLN103 4.2 21.8 1.0
CG A:HIS35 4.3 21.9 1.0
ND1 A:HIS35 4.3 19.7 1.0
CG A:PRO107 4.3 25.0 1.0
C2A A:HEC500 4.3 20.7 1.0
C2C A:HEC500 4.4 20.6 1.0
C2D A:HEC500 4.4 22.4 1.0
C3D A:HEC500 4.4 22.3 1.0
C3C A:HEC500 4.4 23.4 1.0
C3A A:HEC500 4.4 24.3 1.0
C3B A:HEC500 4.4 20.1 1.0
C2B A:HEC500 4.4 25.4 1.0
CB A:PRO107 4.9 25.6 1.0

Iron binding site 2 out of 4 in 3orv

Go back to Iron Binding Sites List in 3orv
Iron binding site 2 out of 4 in the Crystal Structure of the Y294H-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 Y294H-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe600

b:21.5
occ:1.00
FE A:HEC600 0.0 21.5 1.0
NB A:HEC600 2.0 20.9 1.0
NC A:HEC600 2.1 23.0 1.0
ND A:HEC600 2.1 24.4 1.0
NE2 A:HIS205 2.1 21.7 1.0
NA A:HEC600 2.1 23.3 1.0
NE2 A:HIS294 2.1 24.1 1.0
C4B A:HEC600 3.0 20.9 1.0
C1B A:HEC600 3.0 22.1 1.0
C1C A:HEC600 3.0 23.2 1.0
C4C A:HEC600 3.0 19.1 1.0
CD2 A:HIS205 3.0 19.1 1.0
CE1 A:HIS294 3.1 20.8 1.0
C1D A:HEC600 3.1 21.0 1.0
C4A A:HEC600 3.1 21.1 1.0
C4D A:HEC600 3.1 20.8 1.0
CD2 A:HIS294 3.1 24.1 1.0
C1A A:HEC600 3.1 22.5 1.0
CE1 A:HIS205 3.1 20.8 1.0
CHC A:HEC600 3.4 20.8 1.0
CHB A:HEC600 3.4 21.3 1.0
CHD A:HEC600 3.4 18.4 1.0
CHA A:HEC600 3.5 18.9 1.0
ND1 A:HIS294 4.1 21.0 1.0
CG A:HIS294 4.2 23.7 1.0
CG A:HIS205 4.2 23.3 1.0
ND1 A:HIS205 4.2 24.9 1.0
C3B A:HEC600 4.3 19.1 1.0
C2B A:HEC600 4.3 21.0 1.0
C2C A:HEC600 4.3 20.5 1.0
C3C A:HEC600 4.3 20.3 1.0
C3D A:HEC600 4.4 21.1 1.0
C2D A:HEC600 4.4 20.3 1.0
C3A A:HEC600 4.4 23.9 1.0
C2A A:HEC600 4.4 21.6 1.0

Iron binding site 3 out of 4 in 3orv

Go back to Iron Binding Sites List in 3orv
Iron binding site 3 out of 4 in the Crystal Structure of the Y294H-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 Y294H-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe500

b:19.5
occ:1.00
FE B:HEC500 0.0 19.5 1.0
NB B:HEC500 2.0 18.5 1.0
NE2 B:HIS35 2.0 17.0 1.0
ND B:HEC500 2.0 21.2 1.0
NC B:HEC500 2.1 19.2 1.0
NA B:HEC500 2.1 19.6 1.0
CE1 B:HIS35 3.0 17.7 1.0
C1B B:HEC500 3.0 18.9 1.0
C1C B:HEC500 3.0 16.3 1.0
C4C B:HEC500 3.0 21.7 1.0
C1D B:HEC500 3.1 20.6 1.0
CD2 B:HIS35 3.1 16.8 1.0
C1A B:HEC500 3.1 19.3 1.0
C4B B:HEC500 3.1 19.5 1.0
C4D B:HEC500 3.1 20.2 1.0
C4A B:HEC500 3.1 20.1 1.0
CHB B:HEC500 3.4 16.0 1.0
CHD B:HEC500 3.4 18.3 1.0
CHC B:HEC500 3.4 17.7 1.0
CHA B:HEC500 3.5 16.7 1.0
O B:HOH406 3.7 29.5 1.0
NE2 B:GLN103 4.1 18.8 1.0
ND1 B:HIS35 4.1 19.9 1.0
CG B:HIS35 4.2 18.4 1.0
CG B:PRO107 4.3 25.5 1.0
C2B B:HEC500 4.3 14.8 1.0
C2C B:HEC500 4.3 18.1 1.0
C3B B:HEC500 4.3 18.2 1.0
C3C B:HEC500 4.3 18.7 1.0
C2D B:HEC500 4.4 22.2 1.0
C2A B:HEC500 4.4 19.2 1.0
C3A B:HEC500 4.4 18.9 1.0
C3D B:HEC500 4.4 19.6 1.0
CB B:PRO107 4.9 24.6 1.0
CD2 B:LEU70 5.0 19.6 1.0

Iron binding site 4 out of 4 in 3orv

Go back to Iron Binding Sites List in 3orv
Iron binding site 4 out of 4 in the Crystal Structure of the Y294H-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 Y294H-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe600

b:17.9
occ:1.00
FE B:HEC600 0.0 17.9 1.0
NE2 B:HIS205 2.0 18.4 1.0
ND B:HEC600 2.1 19.3 1.0
NC B:HEC600 2.1 18.7 1.0
NB B:HEC600 2.1 18.7 1.0
NA B:HEC600 2.1 17.9 1.0
NE2 B:HIS294 2.1 16.2 1.0
CE1 B:HIS294 3.0 17.4 1.0
CD2 B:HIS205 3.0 15.9 1.0
CE1 B:HIS205 3.0 17.9 1.0
C1A B:HEC600 3.1 16.8 1.0
C1D B:HEC600 3.1 16.7 1.0
C4C B:HEC600 3.1 16.1 1.0
C1C B:HEC600 3.1 14.9 1.0
C4D B:HEC600 3.1 13.7 1.0
C4B B:HEC600 3.1 15.2 1.0
C4A B:HEC600 3.1 16.2 1.0
C1B B:HEC600 3.1 17.4 1.0
CD2 B:HIS294 3.1 17.4 1.0
CHD B:HEC600 3.4 17.0 1.0
CHA B:HEC600 3.5 12.8 1.0
CHB B:HEC600 3.5 16.4 1.0
CHC B:HEC600 3.5 12.7 1.0
ND1 B:HIS294 4.0 17.4 1.0
CG B:HIS294 4.1 17.2 1.0
ND1 B:HIS205 4.1 16.5 1.0
CG B:HIS205 4.2 16.0 1.0
C2D B:HEC600 4.3 19.2 1.0
C3D B:HEC600 4.3 14.5 1.0
C2A B:HEC600 4.4 16.8 1.0
C2C B:HEC600 4.4 17.0 1.0
C3B B:HEC600 4.4 16.6 1.0
C3C B:HEC600 4.4 14.8 1.0
C3A B:HEC600 4.4 16.9 1.0
C2B B:HEC600 4.4 17.4 1.0

Reference:

N.Abu Tarboush, L.M.Jensen, M.Feng, H.Tachikawa, C.M.Wilmot, V.L.Davidson. Functional Importance of Tyrosine 294 and the Catalytic Selectivity For the Bis-Fe(IV) State of Maug Revealed By Replacement of This Axial Heme Ligand with Histidine . Biochemistry V. 49 9783 2010.
ISSN: ISSN 0006-2960
PubMed: 20929212
DOI: 10.1021/BI101254P
Page generated: Sun Aug 4 17:14:37 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy