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Iron in PDB 1d7d: Cytochrome Domain of Cellobiose Dehydrogenase, HP3 Fragment, pH 7.5

Enzymatic activity of Cytochrome Domain of Cellobiose Dehydrogenase, HP3 Fragment, pH 7.5

All present enzymatic activity of Cytochrome Domain of Cellobiose Dehydrogenase, HP3 Fragment, pH 7.5:
1.1.3.25;

Protein crystallography data

The structure of Cytochrome Domain of Cellobiose Dehydrogenase, HP3 Fragment, pH 7.5, PDB code: 1d7d was solved by B.M.Hallberg, T.Bergfors, K.Backbro, C.Divne, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 1.90
Space group P 65
Cell size a, b, c (Å), α, β, γ (°) 138.300, 138.300, 53.390, 90.00, 90.00, 120.00
R / Rfree (%) 18.7 / 22.1

Other elements in 1d7d:

The structure of Cytochrome Domain of Cellobiose Dehydrogenase, HP3 Fragment, pH 7.5 also contains other interesting chemical elements:

Cadmium (Cd) 6 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Cytochrome Domain of Cellobiose Dehydrogenase, HP3 Fragment, pH 7.5 (pdb code 1d7d). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Cytochrome Domain of Cellobiose Dehydrogenase, HP3 Fragment, pH 7.5, PDB code: 1d7d:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1d7d

Go back to Iron Binding Sites List in 1d7d
Iron binding site 1 out of 2 in the Cytochrome Domain of Cellobiose Dehydrogenase, HP3 Fragment, pH 7.5


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome Domain of Cellobiose Dehydrogenase, HP3 Fragment, pH 7.5 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:12.8
occ:1.00
FE A:HEM401 0.0 12.8 1.0
NB A:HEM401 1.9 12.1 1.0
NA A:HEM401 2.0 14.3 1.0
ND A:HEM401 2.0 14.2 1.0
NC A:HEM401 2.0 11.6 1.0
NE2 A:HIS163 2.0 14.1 1.0
SD A:MET65 2.3 16.0 1.0
CD2 A:HIS163 2.9 16.1 1.0
C4B A:HEM401 3.0 10.3 1.0
C1B A:HEM401 3.0 14.0 1.0
C1A A:HEM401 3.0 12.2 1.0
C1C A:HEM401 3.0 11.9 1.0
C4A A:HEM401 3.0 13.7 1.0
C4D A:HEM401 3.1 11.9 1.0
C1D A:HEM401 3.1 12.0 1.0
C4C A:HEM401 3.1 11.7 1.0
CE1 A:HIS163 3.1 14.9 1.0
CHC A:HEM401 3.3 10.6 1.0
CE A:MET65 3.4 11.6 1.0
CHB A:HEM401 3.4 14.8 1.0
CHA A:HEM401 3.4 9.3 1.0
CHD A:HEM401 3.4 11.5 1.0
CG A:MET65 3.5 12.1 1.0
CG A:HIS163 4.1 14.4 1.0
CB A:MET65 4.1 12.2 1.0
ND1 A:HIS163 4.2 13.6 1.0
C2B A:HEM401 4.2 12.2 1.0
C3B A:HEM401 4.2 10.7 1.0
C2A A:HEM401 4.2 14.3 1.0
C3A A:HEM401 4.3 17.4 1.0
C2C A:HEM401 4.3 13.0 1.0
C3D A:HEM401 4.3 12.0 1.0
C2D A:HEM401 4.3 14.2 1.0
C3C A:HEM401 4.3 12.4 1.0
CD1 A:TYR90 4.9 16.0 1.0

Iron binding site 2 out of 2 in 1d7d

Go back to Iron Binding Sites List in 1d7d
Iron binding site 2 out of 2 in the Cytochrome Domain of Cellobiose Dehydrogenase, HP3 Fragment, pH 7.5


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cytochrome Domain of Cellobiose Dehydrogenase, HP3 Fragment, pH 7.5 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe401

b:15.5
occ:1.00
FE B:HEM401 0.0 15.5 1.0
ND B:HEM401 2.0 18.3 1.0
NA B:HEM401 2.0 15.6 1.0
NC B:HEM401 2.0 16.2 1.0
NB B:HEM401 2.0 16.3 1.0
NE2 B:HIS163 2.0 14.3 1.0
SD B:MET65 2.3 18.5 1.0
CD2 B:HIS163 3.0 14.4 1.0
C1B B:HEM401 3.0 16.5 1.0
C4A B:HEM401 3.0 19.7 1.0
C1D B:HEM401 3.0 16.0 1.0
C4D B:HEM401 3.0 15.1 1.0
C1A B:HEM401 3.0 14.3 1.0
C4C B:HEM401 3.0 14.2 1.0
CE1 B:HIS163 3.1 15.8 1.0
C1C B:HEM401 3.1 14.1 1.0
C4B B:HEM401 3.1 14.8 1.0
CE B:MET65 3.3 15.6 1.0
CHB B:HEM401 3.4 17.8 1.0
CHD B:HEM401 3.4 14.7 1.0
CHA B:HEM401 3.4 10.4 1.0
CG B:MET65 3.4 14.2 1.0
CHC B:HEM401 3.5 13.5 1.0
CB B:MET65 4.1 13.3 1.0
ND1 B:HIS163 4.1 15.9 1.0
CG B:HIS163 4.1 15.8 1.0
C3A B:HEM401 4.3 21.1 1.0
C2D B:HEM401 4.3 17.6 1.0
C3D B:HEM401 4.3 17.1 1.0
C2B B:HEM401 4.3 18.8 1.0
C2A B:HEM401 4.3 15.4 1.0
C3C B:HEM401 4.3 13.2 1.0
C3B B:HEM401 4.3 13.0 1.0
C2C B:HEM401 4.3 12.7 1.0
CD1 B:TYR90 4.9 16.2 1.0

Reference:

B.M.Hallberg, T.Bergfors, K.Backbro, G.Pettersson, G.Henriksson, C.Divne. A New Scaffold For Binding Haem in the Cytochrome Domain of the Extracellular Flavocytochrome Cellobiose Dehydrogenase. Structure Fold.Des. V. 8 79 2000.
ISSN: ISSN 0969-2126
PubMed: 10673428
DOI: 10.1016/S0969-2126(00)00082-4
Page generated: Sat Aug 3 03:38:41 2024

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