Atomistry » Iron » PDB 1lrm-1m6m » 1ltd
Atomistry »
  Iron »
    PDB 1lrm-1m6m »
      1ltd »

Iron in PDB 1ltd: The 2.6 Angstroms Refined Structure of the Escherichia Coli Recombinant Saccharomyces Cerevisiae Flavocytochrome B2-Sulphite Complex

Enzymatic activity of The 2.6 Angstroms Refined Structure of the Escherichia Coli Recombinant Saccharomyces Cerevisiae Flavocytochrome B2-Sulphite Complex

All present enzymatic activity of The 2.6 Angstroms Refined Structure of the Escherichia Coli Recombinant Saccharomyces Cerevisiae Flavocytochrome B2-Sulphite Complex:
1.1.2.3;

Protein crystallography data

The structure of The 2.6 Angstroms Refined Structure of the Escherichia Coli Recombinant Saccharomyces Cerevisiae Flavocytochrome B2-Sulphite Complex, PDB code: 1ltd was solved by M.Tegoni, C.Cambillau, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 2.60
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 164.500, 164.500, 114.000, 90.00, 90.00, 120.00
R / Rfree (%) 17.3 / n/a

Iron Binding Sites:

The binding sites of Iron atom in the The 2.6 Angstroms Refined Structure of the Escherichia Coli Recombinant Saccharomyces Cerevisiae Flavocytochrome B2-Sulphite Complex (pdb code 1ltd). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the The 2.6 Angstroms Refined Structure of the Escherichia Coli Recombinant Saccharomyces Cerevisiae Flavocytochrome B2-Sulphite Complex, PDB code: 1ltd:

Iron binding site 1 out of 1 in 1ltd

Go back to Iron Binding Sites List in 1ltd
Iron binding site 1 out of 1 in the The 2.6 Angstroms Refined Structure of the Escherichia Coli Recombinant Saccharomyces Cerevisiae Flavocytochrome B2-Sulphite Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The 2.6 Angstroms Refined Structure of the Escherichia Coli Recombinant Saccharomyces Cerevisiae Flavocytochrome B2-Sulphite Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe560

b:38.3
occ:1.00
FE A:HEM560 0.0 38.3 1.0
NB A:HEM560 1.9 36.5 1.0
NC A:HEM560 2.0 35.2 1.0
ND A:HEM560 2.0 37.6 1.0
NA A:HEM560 2.0 40.5 1.0
NE2 A:HIS66 2.2 38.3 1.0
NE2 A:HIS43 2.2 39.7 1.0
C1D A:HEM560 3.0 37.7 1.0
C4B A:HEM560 3.0 38.2 1.0
C1C A:HEM560 3.0 34.6 1.0
C4C A:HEM560 3.0 33.6 1.0
C4D A:HEM560 3.0 38.7 1.0
C1B A:HEM560 3.0 36.0 1.0
C4A A:HEM560 3.0 39.0 1.0
C1A A:HEM560 3.0 42.9 1.0
CD2 A:HIS43 3.1 40.3 1.0
CD2 A:HIS66 3.1 39.2 1.0
CE1 A:HIS66 3.1 39.6 1.0
CE1 A:HIS43 3.2 41.0 1.0
CHD A:HEM560 3.3 38.0 1.0
CHC A:HEM560 3.4 34.5 1.0
CHB A:HEM560 3.4 36.9 1.0
CHA A:HEM560 3.4 39.0 1.0
C2C A:HEM560 4.2 32.3 1.0
C2D A:HEM560 4.2 36.5 1.0
C3B A:HEM560 4.2 40.3 1.0
C3C A:HEM560 4.2 31.6 1.0
C2B A:HEM560 4.2 36.2 1.0
C3D A:HEM560 4.2 39.7 1.0
CG A:HIS43 4.2 40.7 1.0
CG A:HIS66 4.3 39.5 1.0
ND1 A:HIS66 4.3 40.4 1.0
C3A A:HEM560 4.3 42.4 1.0
C2A A:HEM560 4.3 44.5 1.0
ND1 A:HIS43 4.3 40.6 1.0
CE1 A:PHE62 4.4 40.8 1.0
CD1 A:PHE62 4.8 37.3 1.0

Reference:

M.Tegoni, C.Cambillau. The 2.6-A Refined Structure of the Escherichia Coli Recombinant Saccharomyces Cerevisiae Flavocytochrome B2-Sulfite Complex. Protein Sci. V. 3 303 1994.
ISSN: ISSN 0961-8368
PubMed: 8003966
Page generated: Sat Aug 3 09:55:18 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