Atomistry » Iron » PDB 1uwm-1vme » 1vlb
Atomistry »
  Iron »
    PDB 1uwm-1vme »
      1vlb »

Iron in PDB 1vlb: Structure Refinement of the Aldehyde Oxidoreductase From Desulfovibrio Gigas at 1.28 A

Enzymatic activity of Structure Refinement of the Aldehyde Oxidoreductase From Desulfovibrio Gigas at 1.28 A

All present enzymatic activity of Structure Refinement of the Aldehyde Oxidoreductase From Desulfovibrio Gigas at 1.28 A:
1.2.3.1;

Protein crystallography data

The structure of Structure Refinement of the Aldehyde Oxidoreductase From Desulfovibrio Gigas at 1.28 A, PDB code: 1vlb was solved by J.M.Rebelo, J.M.Dias, R.Huber, J.J.G.Moura, M.J.Romao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.40 / 1.28
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 141.780, 141.780, 160.870, 90.00, 90.00, 120.00
R / Rfree (%) 14.8 / 19.3

Other elements in 1vlb:

The structure of Structure Refinement of the Aldehyde Oxidoreductase From Desulfovibrio Gigas at 1.28 A also contains other interesting chemical elements:

Molybdenum (Mo) 1 atom
Magnesium (Mg) 2 atoms
Chlorine (Cl) 3 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Structure Refinement of the Aldehyde Oxidoreductase From Desulfovibrio Gigas at 1.28 A (pdb code 1vlb). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Structure Refinement of the Aldehyde Oxidoreductase From Desulfovibrio Gigas at 1.28 A, PDB code: 1vlb:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1vlb

Go back to Iron Binding Sites List in 1vlb
Iron binding site 1 out of 4 in the Structure Refinement of the Aldehyde Oxidoreductase From Desulfovibrio Gigas at 1.28 A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure Refinement of the Aldehyde Oxidoreductase From Desulfovibrio Gigas at 1.28 A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe908

b:15.4
occ:1.00
FE1 A:FES908 0.0 15.4 1.0
S2 A:FES908 2.2 16.9 1.0
S1 A:FES908 2.3 16.9 1.0
SG A:CYS100 2.3 16.2 1.0
SG A:CYS139 2.3 16.5 1.0
FE2 A:FES908 2.7 15.9 1.0
CB A:CYS139 3.3 16.1 1.0
CB A:CYS100 3.4 16.2 1.0
N A:CYS100 3.6 16.0 1.0
CA A:CYS100 3.9 15.9 1.0
O A:HOH4105 3.9 17.1 1.0
N A:GLY101 3.9 15.5 1.0
N A:CYS139 4.1 15.2 1.0
CA A:CYS139 4.3 14.9 1.0
C A:CYS100 4.3 18.6 1.0
N A:PHE102 4.4 15.7 1.0
SG A:CYS137 4.4 16.3 1.0
SG A:CYS103 4.7 16.9 1.0
C A:GLN99 4.8 14.5 1.0
CB A:GLN99 4.8 16.1 1.0
N A:ARG138 4.8 16.7 1.0
N A:CYS103 4.9 15.7 1.0
CA A:GLY101 5.0 15.2 1.0

Iron binding site 2 out of 4 in 1vlb

Go back to Iron Binding Sites List in 1vlb
Iron binding site 2 out of 4 in the Structure Refinement of the Aldehyde Oxidoreductase From Desulfovibrio Gigas at 1.28 A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure Refinement of the Aldehyde Oxidoreductase From Desulfovibrio Gigas at 1.28 A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe908

b:15.9
occ:1.00
FE2 A:FES908 0.0 15.9 1.0
S2 A:FES908 2.2 16.9 1.0
S1 A:FES908 2.2 16.9 1.0
SG A:CYS103 2.3 16.9 1.0
SG A:CYS137 2.4 16.3 1.0
FE1 A:FES908 2.7 15.4 1.0
CB A:CYS137 3.4 17.4 1.0
CB A:CYS103 3.4 16.5 1.0
CA A:CYS137 3.8 16.6 1.0
O A:HOH4465 4.1 18.2 1.0
N A:ARG138 4.2 16.7 1.0
N A:CYS103 4.2 15.7 1.0
N A:CYS139 4.3 15.2 1.0
CB A:CYS139 4.3 16.1 1.0
CA A:CYS103 4.4 15.6 1.0
SG A:CYS139 4.4 16.5 1.0
C A:CYS137 4.4 16.7 1.0
CG2 A:THR140 4.6 16.9 1.0
SG A:CYS100 4.6 16.2 1.0
O A:ALA136 4.9 17.8 1.0
CA A:CYS139 4.9 14.9 1.0

Iron binding site 3 out of 4 in 1vlb

Go back to Iron Binding Sites List in 1vlb
Iron binding site 3 out of 4 in the Structure Refinement of the Aldehyde Oxidoreductase From Desulfovibrio Gigas at 1.28 A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure Refinement of the Aldehyde Oxidoreductase From Desulfovibrio Gigas at 1.28 A 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 2.3 18.9 1.0
S1 A:FES909 2.3 18.8 1.0
SG A:CYS45 2.3 18.4 1.0
SG A:CYS40 2.4 19.2 1.0
FE2 A:FES909 2.7 17.0 1.0
CB A:CYS45 3.4 18.3 1.0
N A:CYS40 3.5 18.2 1.0
N A:CYS45 3.5 19.4 1.0
CB A:CYS40 3.6 18.9 1.0
N A:GLU41 3.8 18.6 1.0
CA A:CYS45 3.8 17.8 1.0
CA A:CYS40 3.9 16.7 1.0
N A:GLY46 4.0 17.2 1.0
C A:CYS45 4.2 16.9 1.0
N A:GLN44 4.2 19.9 1.0
C A:CYS40 4.3 18.3 1.0
SG A:CYS60 4.3 18.7 1.0
N A:GLY43 4.4 19.1 1.0
N A:ALA47 4.4 18.0 1.0
C A:GLY39 4.4 18.0 1.0
N A:GLY39 4.5 18.0 1.0
N A:GLN42 4.5 20.7 1.0
C A:GLN44 4.6 17.9 1.0
CA A:GLY39 4.7 18.1 1.0
SG A:CYS48 4.7 17.9 1.0
CA A:GLU41 4.7 18.8 1.0
CA A:GLY43 4.8 19.0 1.0
O A:HOH4200 4.8 23.2 1.0
C A:GLY43 4.9 16.8 1.0
CA A:GLN44 4.9 20.8 1.0
CB A:ALA47 4.9 18.0 1.0
CA A:GLY46 5.0 17.6 1.0

Iron binding site 4 out of 4 in 1vlb

Go back to Iron Binding Sites List in 1vlb
Iron binding site 4 out of 4 in the Structure Refinement of the Aldehyde Oxidoreductase From Desulfovibrio Gigas at 1.28 A


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure Refinement of the Aldehyde Oxidoreductase From Desulfovibrio Gigas at 1.28 A within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe909

b:17.0
occ:1.00
FE2 A:FES909 0.0 17.0 1.0
S1 A:FES909 2.2 18.8 1.0
S2 A:FES909 2.2 18.9 1.0
SG A:CYS60 2.3 18.7 1.0
SG A:CYS48 2.3 17.9 1.0
FE1 A:FES909 2.7 17.1 1.0
CB A:CYS60 3.2 20.3 1.0
CB A:CYS48 3.5 18.9 1.0
N A:CYS60 4.2 18.3 1.0
N A:CYS48 4.3 16.5 1.0
CA A:CYS60 4.3 19.0 1.0
N A:GLY43 4.3 19.1 1.0
CB A:ARG58 4.3 17.9 1.0
SG A:CYS40 4.4 19.2 1.0
CG A:ARG58 4.5 20.7 1.0
CA A:GLY43 4.5 19.0 1.0
CA A:CYS48 4.5 17.3 1.0
SG A:CYS45 4.6 18.4 1.0
N A:GLU41 4.6 18.6 1.0
CA A:GLU41 4.7 18.8 1.0
N A:GLN42 4.9 20.7 1.0
N A:GLY46 4.9 17.2 1.0
N A:ALA47 5.0 18.0 1.0

Reference:

J.M.Rebelo, J.M.Dias, R.Huber, J.J.G.Moura, M.J.Romao. Structure Refinement of the Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop) at 1.28 A J.Biol.Inorg.Chem. V. 6 791 2001.
ISSN: ISSN 0949-8257
PubMed: 11713686
DOI: 10.1007/S007750100255
Page generated: Sat Aug 3 16:14:38 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