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Iron in PDB 2v08: Structure of Wild-Type Phormidium Laminosum Cytochrome C6

Protein crystallography data

The structure of Structure of Wild-Type Phormidium Laminosum Cytochrome C6, PDB code: 2v08 was solved by J.A.R.Worrall, B.G.Schlarb-Ridley, T.Reda, M.J.Marcaida, R.J.Moorlen, J.Wastl, J.Hirst, D.S.Bendall, B.F.Luisi, C.J.Howe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.59 / 2.00
Space group P 63
Cell size a, b, c (Å), α, β, γ (°) 57.364, 57.364, 89.553, 90.00, 90.00, 120.00
R / Rfree (%) 18.4 / 25.5

Other elements in 2v08:

The structure of Structure of Wild-Type Phormidium Laminosum Cytochrome C6 also contains other interesting chemical elements:

Chlorine (Cl) 3 atoms
Zinc (Zn) 9 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Wild-Type Phormidium Laminosum Cytochrome C6 (pdb code 2v08). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of Wild-Type Phormidium Laminosum Cytochrome C6, PDB code: 2v08:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 2v08

Go back to Iron Binding Sites List in 2v08
Iron binding site 1 out of 2 in the Structure of Wild-Type Phormidium Laminosum Cytochrome C6


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Wild-Type Phormidium Laminosum Cytochrome C6 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1087

b:19.9
occ:1.00
FE A:HEC1087 0.0 19.9 1.0
NA A:HEC1087 2.0 12.3 1.0
NE2 A:HIS19 2.0 8.5 1.0
NB A:HEC1087 2.0 10.1 1.0
ND A:HEC1087 2.1 11.7 1.0
NC A:HEC1087 2.1 11.6 1.0
SD A:MET59 2.5 18.6 1.0
CE1 A:HIS19 3.0 9.0 1.0
C1B A:HEC1087 3.0 9.4 1.0
CD2 A:HIS19 3.0 6.6 1.0
C4A A:HEC1087 3.0 10.1 1.0
C1A A:HEC1087 3.0 11.6 1.0
C4D A:HEC1087 3.0 12.6 1.0
C4B A:HEC1087 3.0 10.4 1.0
C1D A:HEC1087 3.1 11.3 1.0
C1C A:HEC1087 3.1 8.7 1.0
C4C A:HEC1087 3.1 13.2 1.0
CHC A:HEC1087 3.4 10.7 1.0
CHB A:HEC1087 3.4 10.5 1.0
CHA A:HEC1087 3.4 10.1 1.0
CHD A:HEC1087 3.5 11.4 1.0
CG A:MET59 3.5 19.3 1.0
CE A:MET59 3.6 17.3 1.0
CB A:MET59 4.1 17.6 1.0
ND1 A:HIS19 4.1 9.3 1.0
CG A:HIS19 4.2 8.7 1.0
C3A A:HEC1087 4.2 10.9 1.0
C2B A:HEC1087 4.2 11.0 1.0
C2A A:HEC1087 4.2 12.5 1.0
C3D A:HEC1087 4.2 11.4 1.0
C2D A:HEC1087 4.3 11.7 1.0
C3B A:HEC1087 4.3 10.8 1.0
C2C A:HEC1087 4.3 12.6 1.0
C3C A:HEC1087 4.3 12.0 1.0

Iron binding site 2 out of 2 in 2v08

Go back to Iron Binding Sites List in 2v08
Iron binding site 2 out of 2 in the Structure of Wild-Type Phormidium Laminosum Cytochrome C6


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Wild-Type Phormidium Laminosum Cytochrome C6 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1087

b:26.5
occ:1.00
FE B:HEC1087 0.0 26.5 1.0
ND B:HEC1087 2.0 18.8 1.0
NE2 B:HIS19 2.0 12.1 1.0
NC B:HEC1087 2.1 17.8 1.0
NB B:HEC1087 2.1 23.1 1.0
NA B:HEC1087 2.1 21.0 1.0
SD B:MET59 2.3 23.2 1.0
CE1 B:HIS19 2.9 13.7 1.0
C1D B:HEC1087 3.0 19.2 1.0
C4C B:HEC1087 3.0 20.9 1.0
C4D B:HEC1087 3.0 21.0 1.0
C1C B:HEC1087 3.1 21.3 1.0
C4B B:HEC1087 3.1 21.1 1.0
CD2 B:HIS19 3.1 13.2 1.0
C1B B:HEC1087 3.1 21.8 1.0
C4A B:HEC1087 3.1 23.0 1.0
C1A B:HEC1087 3.1 21.4 1.0
CHD B:HEC1087 3.3 18.9 1.0
CE B:MET59 3.4 26.4 1.0
CHC B:HEC1087 3.4 18.9 1.0
CHA B:HEC1087 3.5 19.9 1.0
CHB B:HEC1087 3.5 21.1 1.0
CG B:MET59 3.6 24.9 1.0
CB B:MET59 4.0 24.5 1.0
ND1 B:HIS19 4.0 13.5 1.0
C2D B:HEC1087 4.2 19.4 1.0
CG B:HIS19 4.2 14.9 1.0
C3D B:HEC1087 4.2 18.9 1.0
C3C B:HEC1087 4.3 16.5 1.0
C2C B:HEC1087 4.3 19.4 1.0
C3B B:HEC1087 4.3 23.6 1.0
C2B B:HEC1087 4.4 22.9 1.0
C3A B:HEC1087 4.4 22.3 1.0
C2A B:HEC1087 4.4 19.9 1.0
CA B:MET59 5.0 24.4 1.0

Reference:

J.A.Worrall, B.G.Schlarb-Ridley, T.Reda, M.J.Marcaida, R.J.Moorlen, J.Wastl, J.Hirst, D.S.Bendall, B.F.Luisi, C.J.Howe. Modulation of Heme Redox Potential in the Cytochrome C6 Family. J. Am. Chem. Soc. V. 129 9468 2007.
ISSN: ISSN 0002-7863
PubMed: 17625855
DOI: 10.1021/JA072346G
Page generated: Sun Aug 4 02:24:10 2024

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