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Iron in PDB 1c2r: Molecular Structure of Cytochrome C2 Isolated From Rhodobacter Capsulatus Determined at 2.5 Angstroms Resolution

Protein crystallography data

The structure of Molecular Structure of Cytochrome C2 Isolated From Rhodobacter Capsulatus Determined at 2.5 Angstroms Resolution, PDB code: 1c2r was solved by M.M.Benning, G.Wesenberg, M.S.Caffrey, R.G.Bartsch, T.E.Meyer, M.A.Cusanovich, I.Rayment, H.M.Holden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.50
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 100.030, 100.030, 162.100, 90.00, 90.00, 120.00
R / Rfree (%) n/a / n/a

Iron Binding Sites:

The binding sites of Iron atom in the Molecular Structure of Cytochrome C2 Isolated From Rhodobacter Capsulatus Determined at 2.5 Angstroms Resolution (pdb code 1c2r). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Molecular Structure of Cytochrome C2 Isolated From Rhodobacter Capsulatus Determined at 2.5 Angstroms Resolution, PDB code: 1c2r:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1c2r

Go back to Iron Binding Sites List in 1c2r
Iron binding site 1 out of 2 in the Molecular Structure of Cytochrome C2 Isolated From Rhodobacter Capsulatus Determined at 2.5 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Molecular Structure of Cytochrome C2 Isolated From Rhodobacter Capsulatus Determined at 2.5 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe120

b:18.1
occ:1.00
FE A:HEM120 0.0 18.1 1.0
NA A:HEM120 1.9 4.3 1.0
NB A:HEM120 1.9 9.3 1.0
NC A:HEM120 1.9 17.1 1.0
ND A:HEM120 2.0 3.9 1.0
NE2 A:HIS17 2.1 15.1 1.0
SD A:MET96 2.3 17.0 1.0
C4B A:HEM120 2.9 15.9 1.0
C1A A:HEM120 2.9 13.0 1.0
C1B A:HEM120 3.0 10.3 1.0
C4C A:HEM120 3.0 25.4 1.0
C4D A:HEM120 3.0 15.5 1.0
C1D A:HEM120 3.0 21.7 1.0
CD2 A:HIS17 3.0 21.0 1.0
C4A A:HEM120 3.0 20.2 1.0
C1C A:HEM120 3.0 15.5 1.0
CE1 A:HIS17 3.1 17.6 1.0
CHD A:HEM120 3.3 19.0 1.0
CHA A:HEM120 3.3 27.9 1.0
CHC A:HEM120 3.3 13.6 1.0
CE A:MET96 3.4 11.9 1.0
CG A:MET96 3.4 5.4 1.0
CHB A:HEM120 3.4 35.7 1.0
C3B A:HEM120 4.1 10.4 1.0
C2B A:HEM120 4.1 17.6 1.0
CG A:HIS17 4.2 13.8 1.0
C2A A:HEM120 4.2 9.8 1.0
C3D A:HEM120 4.2 7.4 1.0
ND1 A:HIS17 4.2 17.4 1.0
C2D A:HEM120 4.2 3.2 1.0
C3C A:HEM120 4.2 21.4 1.0
C3A A:HEM120 4.2 10.4 1.0
CB A:MET96 4.3 14.1 1.0
C2C A:HEM120 4.3 14.4 1.0

Iron binding site 2 out of 2 in 1c2r

Go back to Iron Binding Sites List in 1c2r
Iron binding site 2 out of 2 in the Molecular Structure of Cytochrome C2 Isolated From Rhodobacter Capsulatus Determined at 2.5 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Molecular Structure of Cytochrome C2 Isolated From Rhodobacter Capsulatus Determined at 2.5 Angstroms Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe120

b:19.3
occ:1.00
FE B:HEM120 0.0 19.3 1.0
NE2 B:HIS17 1.9 15.8 1.0
NC B:HEM120 1.9 24.9 1.0
NB B:HEM120 2.0 2.5 1.0
ND B:HEM120 2.0 1.0 1.0
NA B:HEM120 2.0 7.2 1.0
SD B:MET96 2.2 18.3 1.0
CD2 B:HIS17 2.9 28.9 1.0
CE1 B:HIS17 2.9 28.9 1.0
C4B B:HEM120 2.9 34.4 1.0
C1C B:HEM120 3.0 20.2 1.0
C1D B:HEM120 3.0 18.9 1.0
C1B B:HEM120 3.0 34.0 1.0
C4D B:HEM120 3.0 28.4 1.0
C4A B:HEM120 3.0 25.4 1.0
C4C B:HEM120 3.0 24.4 1.0
C1A B:HEM120 3.1 18.1 1.0
CG B:MET96 3.2 3.2 1.0
CHC B:HEM120 3.3 2.5 1.0
CHD B:HEM120 3.3 13.0 1.0
CHB B:HEM120 3.4 14.1 1.0
CHA B:HEM120 3.4 7.0 1.0
CE B:MET96 3.4 18.0 1.0
ND1 B:HIS17 4.1 14.1 1.0
CG B:HIS17 4.1 17.4 1.0
C3B B:HEM120 4.2 23.9 1.0
CB B:MET96 4.2 18.7 1.0
C2D B:HEM120 4.2 11.0 1.0
C2C B:HEM120 4.2 15.4 1.0
C2B B:HEM120 4.2 40.3 1.0
C3D B:HEM120 4.3 5.0 1.0
C3C B:HEM120 4.3 26.7 1.0
C2A B:HEM120 4.3 22.1 1.0
C3A B:HEM120 4.3 17.4 1.0

Reference:

M.M.Benning, G.Wesenberg, M.S.Caffrey, R.G.Bartsch, T.E.Meyer, M.A.Cusanovich, I.Rayment, H.M.Holden. Molecular Structure of Cytochrome C2 Isolated From Rhodobacter Capsulatus Determined at 2.5 A Resolution. J.Mol.Biol. V. 220 673 1991.
ISSN: ISSN 0022-2836
PubMed: 1651396
DOI: 10.1016/0022-2836(91)90109-J
Page generated: Sun Dec 13 14:08:21 2020

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