Iron in PDB 1jgc: The 2.6 A Structure Resolution of Rhodobacter Capsulatus Bacterioferritin with Metal-Free Dinuclear Site and Heme Iron in A Crystallographic Special Position

The structure of The 2.6 A Structure Resolution of Rhodobacter Capsulatus Bacterioferritin with Metal-Free Dinuclear Site and Heme Iron in A Crystallographic Special Position, PDB code: 1jgc was solved by D.Cobessi, L.-S.Huang, M.Ban, N.G.Pon, F.Daldal, E.A.Berry, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	21.44 / 2.60
Space group	I 4 2 2
Cell size a, b, c (Å), α, β, γ (°)	142.370, 142.370, 140.880, 90.00, 90.00, 90.00
R / Rfree (%)	22.5 / 24.2

The binding sites of Iron atom in the The 2.6 A Structure Resolution of Rhodobacter Capsulatus Bacterioferritin with Metal-Free Dinuclear Site and Heme Iron in A Crystallographic Special Position (pdb code 1jgc). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the The 2.6 A Structure Resolution of Rhodobacter Capsulatus Bacterioferritin with Metal-Free Dinuclear Site and Heme Iron in A Crystallographic Special Position, PDB code: 1jgc:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the The 2.6 A Structure Resolution of Rhodobacter Capsulatus Bacterioferritin with Metal-Free Dinuclear Site and Heme Iron in A Crystallographic Special Position


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 A Structure Resolution of Rhodobacter Capsulatus Bacterioferritin with Metal-Free Dinuclear Site and Heme Iron in A Crystallographic Special Position within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:24.6 occ:0.50 FE A:HEM201 0.0 24.6 0.5 NA A:HEM201 2.0 26.9 0.5 NC A:HEM201 2.0 25.5 0.5 NB A:HEM201 2.0 26.2 0.5 ND A:HEM201 2.0 25.8 0.5 SD A:MET52 2.6 23.3 1.0 C1A A:HEM201 3.0 27.2 0.5 C1C A:HEM201 3.0 25.5 0.5 C4A A:HEM201 3.0 27.1 0.5 C4B A:HEM201 3.1 26.0 0.5 C4D A:HEM201 3.1 26.2 0.5 C4C A:HEM201 3.1 25.5 0.5 C1D A:HEM201 3.1 25.4 0.5 C1B A:HEM201 3.1 26.7 0.5 CHC A:HEM201 3.4 25.8 0.5 CHA A:HEM201 3.4 26.6 0.5 CHB A:HEM201 3.4 26.7 0.5 CHD A:HEM201 3.4 25.0 0.5 CG A:MET52 3.7 24.3 1.0 CE A:MET52 3.8 24.9 1.0 C2A A:HEM201 4.1 28.5 0.5 C3A A:HEM201 4.2 28.2 0.5 C2C A:HEM201 4.3 26.0 0.5 C3C A:HEM201 4.3 25.2 0.5 C3D A:HEM201 4.3 26.7 0.5 C2B A:HEM201 4.3 26.9 0.5 C2D A:HEM201 4.3 25.9 0.5 C3B A:HEM201 4.3 26.4 0.5 CB A:MET52 4.5 23.7 1.0

Iron binding site 2 out of 3 in the The 2.6 A Structure Resolution of Rhodobacter Capsulatus Bacterioferritin with Metal-Free Dinuclear Site and Heme Iron in A Crystallographic Special Position


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The 2.6 A Structure Resolution of Rhodobacter Capsulatus Bacterioferritin with Metal-Free Dinuclear Site and Heme Iron in A Crystallographic Special Position within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe200 b:26.7 occ:0.50 FE B:HEM200 0.0 26.7 0.5 NC B:HEM200 1.9 27.9 0.5 NA B:HEM200 2.0 28.5 0.5 NB B:HEM200 2.0 28.3 0.5 ND B:HEM200 2.0 27.9 0.5 SD B:MET52 2.6 22.3 1.0 C1C B:HEM200 3.0 27.9 0.5 C4C B:HEM200 3.0 28.2 0.5 C4A B:HEM200 3.1 28.8 0.5 C4B B:HEM200 3.1 27.8 0.5 C1A B:HEM200 3.1 28.9 0.5 C1D B:HEM200 3.1 27.9 0.5 C1B B:HEM200 3.1 28.4 0.5 C4D B:HEM200 3.1 27.8 0.5 CHC B:HEM200 3.3 28.0 0.5 CHD B:HEM200 3.4 28.0 0.5 CHB B:HEM200 3.4 28.6 0.5 CHA B:HEM200 3.4 28.3 0.5 CG B:MET52 3.7 22.1 1.0 CE B:MET52 3.8 22.5 1.0 C2C B:HEM200 4.2 28.3 0.5 C3C B:HEM200 4.2 28.5 0.5 C2A B:HEM200 4.3 30.1 0.5 C3A B:HEM200 4.3 29.6 0.5 C2B B:HEM200 4.3 28.1 0.5 C3B B:HEM200 4.3 28.1 0.5 C2D B:HEM200 4.3 28.3 0.5 C3D B:HEM200 4.4 28.1 0.5 CB B:MET52 4.5 22.9 1.0

Iron binding site 3 out of 3 in the The 2.6 A Structure Resolution of Rhodobacter Capsulatus Bacterioferritin with Metal-Free Dinuclear Site and Heme Iron in A Crystallographic Special Position


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of The 2.6 A Structure Resolution of Rhodobacter Capsulatus Bacterioferritin with Metal-Free Dinuclear Site and Heme Iron in A Crystallographic Special Position within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe202 b:26.4 occ:0.50 FE C:HEM202 0.0 26.4 0.5 NB C:HEM202 2.0 27.0 0.5 NC C:HEM202 2.0 26.9 0.5 ND C:HEM202 2.0 27.4 0.5 NA C:HEM202 2.0 27.7 0.5 SD C:MET52 2.5 26.4 1.0 C1C C:HEM202 3.0 26.7 0.5 C4B C:HEM202 3.0 26.8 0.5 C4D C:HEM202 3.1 28.2 0.5 C1A C:HEM202 3.1 28.3 0.5 C1B C:HEM202 3.1 27.2 0.5 C4A C:HEM202 3.1 28.1 0.5 C4C C:HEM202 3.1 27.2 0.5 C1D C:HEM202 3.1 27.7 0.5 CHC C:HEM202 3.4 26.6 0.5 CHA C:HEM202 3.4 27.6 0.5 CHB C:HEM202 3.5 27.4 0.5 CHD C:HEM202 3.5 27.5 0.5 CG C:MET52 3.5 24.8 1.0 CE C:MET52 3.7 24.5 1.0 C2C C:HEM202 4.3 27.0 0.5 CB C:MET52 4.3 24.9 1.0 C3B C:HEM202 4.3 26.9 0.5 C3A C:HEM202 4.3 28.6 0.5 C2A C:HEM202 4.3 29.0 0.5 C3C C:HEM202 4.3 26.8 0.5 C3D C:HEM202 4.3 28.4 0.5 C2B C:HEM202 4.3 26.9 0.5 C2D C:HEM202 4.3 28.2 0.5

D.Cobessi, L.S.Huang, M.Ban, N.G.Pon, F.Daldal, E.A.Berry. The 2.6 A Resolution Structure of Rhodobacter Capsulatus Bacterioferritin with Metal-Free Dinuclear Site and Heme Iron in A Crystallographic 'Special Position'. Acta Crystallogr.,Sect.D V. 58 29 2002.
ISSN: ISSN 0907-4449
PubMed: 11752777
DOI: 10.1107/S0907444901017267