Iron in PDB 1lm3: A Multi-Generation Analysis of Cytochrome B562 Redox Variants: Evolutionary Strategies For Modulating Redox Potential Revealed Using A Library Approach

The structure of A Multi-Generation Analysis of Cytochrome B562 Redox Variants: Evolutionary Strategies For Modulating Redox Potential Revealed Using A Library Approach, PDB code: 1lm3 was solved by S.L.Springs, S.E.Bass, G.Bowman, I.Nodelman, C.E.Schutt, G.L.Mclendon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	42.098, 48.995, 114.419, 90.00, 90.00, 90.00
R / Rfree (%)	23.2 / 33.3

The structure of A Multi-Generation Analysis of Cytochrome B562 Redox Variants: Evolutionary Strategies For Modulating Redox Potential Revealed Using A Library Approach also contains other interesting chemical elements:

Magnesium

(Mg)

3 atoms

The binding sites of Iron atom in the A Multi-Generation Analysis of Cytochrome B562 Redox Variants: Evolutionary Strategies For Modulating Redox Potential Revealed Using A Library Approach (pdb code 1lm3). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the A Multi-Generation Analysis of Cytochrome B562 Redox Variants: Evolutionary Strategies For Modulating Redox Potential Revealed Using A Library Approach, PDB code: 1lm3:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the A Multi-Generation Analysis of Cytochrome B562 Redox Variants: Evolutionary Strategies For Modulating Redox Potential Revealed Using A Library Approach


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of A Multi-Generation Analysis of Cytochrome B562 Redox Variants: Evolutionary Strategies For Modulating Redox Potential Revealed Using A Library Approach within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe200 b:51.1 occ:1.00 FE B:HEM200 0.0 51.1 1.0 NB B:HEM200 1.9 50.3 1.0 NA B:HEM200 2.0 51.5 1.0 ND B:HEM200 2.0 51.0 1.0 NC B:HEM200 2.0 50.8 1.0 NE2 B:HIS102 2.2 28.3 1.0 SD B:MET7 2.4 25.3 1.0 C4A B:HEM200 3.0 52.2 1.0 C1A B:HEM200 3.0 52.7 1.0 C4D B:HEM200 3.0 52.3 1.0 C1B B:HEM200 3.0 49.8 1.0 C4B B:HEM200 3.0 50.2 1.0 C1C B:HEM200 3.0 50.8 1.0 C4C B:HEM200 3.0 50.3 1.0 C1D B:HEM200 3.0 51.3 1.0 CE1 B:HIS102 3.1 28.3 1.0 CD2 B:HIS102 3.2 28.8 1.0 CHA B:HEM200 3.4 52.8 1.0 CHB B:HEM200 3.4 50.7 1.0 CHC B:HEM200 3.4 51.1 1.0 CHD B:HEM200 3.4 50.9 1.0 CG B:MET7 3.4 26.1 1.0 CE B:MET7 3.9 26.7 1.0 CB B:MET7 4.1 25.2 1.0 ND1 B:HIS102 4.2 29.8 1.0 C3B B:HEM200 4.3 50.5 1.0 C3A B:HEM200 4.3 53.4 1.0 C2A B:HEM200 4.3 54.4 1.0 C3D B:HEM200 4.3 53.1 1.0 C2B B:HEM200 4.3 49.9 1.0 C2C B:HEM200 4.3 51.1 1.0 C3C B:HEM200 4.3 51.2 1.0 C2D B:HEM200 4.3 52.6 1.0 CG B:HIS102 4.3 28.9 1.0 CA B:MET7 4.9 15.9 1.0 CG B:ARG98 5.0 49.6 1.0

Iron binding site 2 out of 2 in the A Multi-Generation Analysis of Cytochrome B562 Redox Variants: Evolutionary Strategies For Modulating Redox Potential Revealed Using A Library Approach


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of A Multi-Generation Analysis of Cytochrome B562 Redox Variants: Evolutionary Strategies For Modulating Redox Potential Revealed Using A Library Approach within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe200 b:51.1 occ:1.00 FE D:HEM200 0.0 51.1 1.0 NA D:HEM200 1.9 51.5 1.0 NB D:HEM200 2.0 50.3 1.0 ND D:HEM200 2.0 51.0 1.0 NC D:HEM200 2.0 50.8 1.0 NE2 D:HIS102 2.1 33.4 1.0 SD D:MET7 2.4 21.4 1.0 CE1 D:HIS102 2.9 33.3 1.0 C1A D:HEM200 3.0 52.7 1.0 C4A D:HEM200 3.0 52.2 1.0 C4D D:HEM200 3.0 52.3 1.0 C4B D:HEM200 3.0 50.2 1.0 C1B D:HEM200 3.0 49.8 1.0 C1C D:HEM200 3.0 50.8 1.0 C1D D:HEM200 3.0 51.3 1.0 C4C D:HEM200 3.0 50.3 1.0 CD2 D:HIS102 3.2 33.8 1.0 CG D:MET7 3.3 22.2 1.0 CHA D:HEM200 3.3 52.8 1.0 CHB D:HEM200 3.4 50.7 1.0 CHC D:HEM200 3.4 51.1 1.0 CHD D:HEM200 3.4 50.9 1.0 CE D:MET7 3.7 22.7 1.0 CB D:MET7 4.1 21.3 1.0 ND1 D:HIS102 4.1 34.8 1.0 C2A D:HEM200 4.2 54.4 1.0 C3A D:HEM200 4.2 53.4 1.0 C3B D:HEM200 4.3 50.5 1.0 C2B D:HEM200 4.3 49.9 1.0 C3D D:HEM200 4.3 53.1 1.0 CG D:HIS102 4.3 33.9 1.0 C2C D:HEM200 4.3 51.1 1.0 C3C D:HEM200 4.3 51.2 1.0 C2D D:HEM200 4.3 52.6 1.0 CG D:ARG98 4.6 15.8 1.0 CD1 D:LEU10 4.9 38.4 1.0 CA D:MET7 5.0 30.5 1.0

S.L.Springs, S.E.Bass, G.Bowman, I.Nodelman, C.E.Schutt, G.L.Mclendon. A Multigeneration Analysis of Cytochrome B(562) Redox Variants: Evolutionary Strategies For Modulating Redox Potential Revealed Using A Library Approach. Biochemistry V. 41 4321 2002.
ISSN: ISSN 0006-2960
PubMed: 11914078
DOI: 10.1021/BI012066S