Atomistry » Iron » PDB 3etr-3fou » 3fah
Atomistry »
  Iron »
    PDB 3etr-3fou »
      3fah »

Iron in PDB 3fah: Glycerol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas

Enzymatic activity of Glycerol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas

All present enzymatic activity of Glycerol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas:
1.2.99.7;

Protein crystallography data

The structure of Glycerol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas, PDB code: 3fah was solved by T.Santos-Silva, M.J.Romao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.98 / 1.72
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 142.560, 142.560, 161.880, 90.00, 90.00, 120.00
R / Rfree (%) 16 / 19.1

Other elements in 3fah:

The structure of Glycerol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas also contains other interesting chemical elements:

Molybdenum (Mo) 1 atom
Magnesium (Mg) 3 atoms
Chlorine (Cl) 3 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Glycerol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas (pdb code 3fah). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Glycerol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas, PDB code: 3fah:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 3fah

Go back to Iron Binding Sites List in 3fah
Iron binding site 1 out of 4 in the Glycerol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Glycerol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe908

b:13.4
occ:1.00
FE1 A:FES908 0.0 13.4 1.0
S2 A:FES908 2.2 15.6 1.0
S1 A:FES908 2.2 14.7 1.0
SG A:CYS100 2.3 25.6 1.0
SG A:CYS139 2.4 26.7 1.0
FE2 A:FES908 2.7 13.9 1.0
CB A:CYS139 3.2 24.5 1.0
CB A:CYS100 3.4 24.6 1.0
N A:CYS100 3.7 24.8 1.0
O A:HOH1221 3.9 12.7 1.0
N A:GLY101 3.9 24.9 1.0
CA A:CYS100 4.0 25.1 1.0
N A:CYS139 4.2 23.8 1.0
CA A:CYS139 4.3 23.6 1.0
C A:CYS100 4.3 25.1 1.0
SG A:CYS137 4.4 25.5 1.0
N A:PHE102 4.4 25.1 1.0
SG A:CYS103 4.6 27.5 1.0
C A:GLN99 4.8 24.8 1.0
CB A:GLN99 4.8 23.5 1.0
N A:ARG138 4.9 23.9 1.0
N A:CYS103 4.9 24.7 1.0
CA A:GLY101 5.0 25.6 1.0

Iron binding site 2 out of 4 in 3fah

Go back to Iron Binding Sites List in 3fah
Iron binding site 2 out of 4 in the Glycerol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Glycerol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe908

b:13.9
occ:1.00
FE2 A:FES908 0.0 13.9 1.0
S1 A:FES908 2.2 14.7 1.0
S2 A:FES908 2.2 15.6 1.0
SG A:CYS103 2.2 27.5 1.0
SG A:CYS137 2.4 25.5 1.0
FE1 A:FES908 2.7 13.4 1.0
CB A:CYS137 3.3 25.5 1.0
CB A:CYS103 3.4 24.7 1.0
CA A:CYS137 3.7 25.5 1.0
O A:HOH1229 4.1 14.1 1.0
N A:ARG138 4.2 23.9 1.0
N A:CYS103 4.2 24.7 1.0
CB A:CYS139 4.2 24.5 1.0
N A:CYS139 4.4 23.8 1.0
CA A:CYS103 4.4 25.3 1.0
C A:CYS137 4.4 24.8 1.0
SG A:CYS139 4.5 26.7 1.0
CG2 A:THR140 4.7 25.5 1.0
SG A:CYS100 4.7 25.6 1.0
O A:ALA136 4.8 25.0 1.0
CA A:CYS139 4.9 23.6 1.0

Iron binding site 3 out of 4 in 3fah

Go back to Iron Binding Sites List in 3fah
Iron binding site 3 out of 4 in the Glycerol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Glycerol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe909

b:17.1
occ:1.00
FE1 A:FES909 0.0 17.1 1.0
S2 A:FES909 2.2 18.4 1.0
S1 A:FES909 2.2 18.5 1.0
SG A:CYS45 2.3 25.7 1.0
SG A:CYS40 2.4 26.9 1.0
FE2 A:FES909 2.8 16.6 1.0
CB A:CYS45 3.4 24.1 1.0
N A:CYS45 3.5 24.9 1.0
N A:CYS40 3.5 25.8 1.0
CB A:CYS40 3.6 25.6 1.0
CA A:CYS45 3.8 24.4 1.0
N A:GLU41 3.8 24.8 1.0
N A:GLY46 4.0 23.6 1.0
CA A:CYS40 4.0 25.2 1.0
N A:GLN44 4.2 25.1 1.0
C A:CYS45 4.2 23.7 1.0
SG A:CYS60 4.3 25.4 1.0
N A:ALA47 4.4 23.4 1.0
C A:CYS40 4.4 25.5 1.0
N A:GLY39 4.4 23.8 1.0
N A:GLY43 4.5 25.4 1.0
C A:GLY39 4.5 25.1 1.0
O A:HOH1332 4.6 25.4 1.0
C A:GLN44 4.6 25.2 1.0
N A:GLN42 4.6 25.3 1.0
SG A:CYS48 4.7 24.4 1.0
CA A:GLY39 4.7 25.1 1.0
CA A:GLU41 4.8 25.7 1.0
C A:GLY43 4.8 25.6 1.0
CA A:GLY43 4.8 25.8 1.0
CB A:ALA47 4.9 23.7 1.0
CA A:GLY46 4.9 23.7 1.0
CA A:GLN44 4.9 25.4 1.0

Iron binding site 4 out of 4 in 3fah

Go back to Iron Binding Sites List in 3fah
Iron binding site 4 out of 4 in the Glycerol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Glycerol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe909

b:16.6
occ:1.00
FE2 A:FES909 0.0 16.6 1.0
S1 A:FES909 2.2 18.5 1.0
S2 A:FES909 2.2 18.4 1.0
SG A:CYS48 2.3 24.4 1.0
SG A:CYS60 2.3 25.4 1.0
FE1 A:FES909 2.8 17.1 1.0
CB A:CYS60 3.2 24.6 1.0
CB A:CYS48 3.4 23.8 1.0
N A:CYS60 4.2 24.1 1.0
N A:CYS48 4.2 23.8 1.0
CA A:CYS60 4.3 24.6 1.0
CB A:ARG58 4.4 23.9 1.0
N A:GLY43 4.4 25.4 1.0
CA A:CYS48 4.5 23.6 1.0
CG A:ARG58 4.5 25.2 1.0
SG A:CYS40 4.5 26.9 1.0
CA A:GLY43 4.5 25.8 1.0
SG A:CYS45 4.6 25.7 1.0
N A:GLU41 4.6 24.8 1.0
CA A:GLU41 4.7 25.7 1.0
N A:ALA47 4.9 23.4 1.0
N A:GLY46 4.9 23.6 1.0
N A:GLN42 4.9 25.3 1.0

Reference:

T.Santos-Silva, F.Ferroni, A.Thapper, J.Marangon, P.J.Gonzalez, A.C.Rizzi, I.Moura, J.J.Moura, M.J.Romao, C.D.Brondino. Kinetic, Structural, and Epr Studies Reveal That Aldehyde Oxidoreductase From Desulfovibrio Gigas Does Not Need A Sulfido Ligand For Catalysis and Give Evidence For A Direct Mo-C Interaction in A Biological System. J.Am.Chem.Soc. V. 131 7990 2009.
ISSN: ISSN 0002-7863
PubMed: 19459677
DOI: 10.1021/JA809448R
Page generated: Sun Dec 13 15:05:30 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy