Iron in PDB 3l1m: Crystal Structure of A Ni-Directed Dimer of Cytochrome CB562 with A Quinolate-Histidine Hybrid Coordination Motif

The structure of Crystal Structure of A Ni-Directed Dimer of Cytochrome CB562 with A Quinolate-Histidine Hybrid Coordination Motif, PDB code: 3l1m was solved by R.J.Radford, F.A.Tezcan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.30
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	88.440, 34.511, 46.896, 90.00, 90.00, 90.00
R / Rfree (%)	26.6 / 31.4

The structure of Crystal Structure of A Ni-Directed Dimer of Cytochrome CB562 with A Quinolate-Histidine Hybrid Coordination Motif also contains other interesting chemical elements:

Nickel

(Ni)

1 atom

The binding sites of Iron atom in the Crystal Structure of A Ni-Directed Dimer of Cytochrome CB562 with A Quinolate-Histidine Hybrid Coordination Motif (pdb code 3l1m). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of A Ni-Directed Dimer of Cytochrome CB562 with A Quinolate-Histidine Hybrid Coordination Motif, PDB code: 3l1m:

Iron binding site 1 out of 1 in the Crystal Structure of A Ni-Directed Dimer of Cytochrome CB562 with A Quinolate-Histidine Hybrid Coordination Motif


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of A Ni-Directed Dimer of Cytochrome CB562 with A Quinolate-Histidine Hybrid Coordination Motif within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe150 b:22.6 occ:1.00 FE A:HEM150 0.0 22.6 1.0 NC A:HEM150 2.0 23.1 1.0 NB A:HEM150 2.0 23.9 1.0 ND A:HEM150 2.0 28.4 1.0 NA A:HEM150 2.0 27.7 1.0 NE2 A:HIS102 2.1 24.4 1.0 SD A:MET7 2.2 27.7 1.0 CD2 A:HIS102 3.0 25.3 1.0 C1C A:HEM150 3.0 19.4 1.0 C4B A:HEM150 3.0 20.2 1.0 C4C A:HEM150 3.0 24.3 1.0 C4D A:HEM150 3.1 29.1 1.0 C1D A:HEM150 3.1 28.7 1.0 C1B A:HEM150 3.1 23.0 1.0 C4A A:HEM150 3.1 27.9 1.0 CE1 A:HIS102 3.1 25.6 1.0 C1A A:HEM150 3.1 30.2 1.0 CHC A:HEM150 3.4 17.3 1.0 CHD A:HEM150 3.4 26.7 1.0 CE A:MET7 3.4 23.7 1.0 CG A:MET7 3.5 25.1 1.0 CHB A:HEM150 3.5 24.4 1.0 CHA A:HEM150 3.5 28.1 1.0 CG A:HIS102 4.2 29.7 1.0 ND1 A:HIS102 4.2 27.2 1.0 CB A:MET7 4.2 21.4 1.0 C2C A:HEM150 4.3 19.9 1.0 C3D A:HEM150 4.3 31.3 1.0 C3C A:HEM150 4.3 23.1 1.0 C3B A:HEM150 4.3 21.1 1.0 C2B A:HEM150 4.3 22.0 1.0 C2D A:HEM150 4.3 31.7 1.0 C3A A:HEM150 4.3 30.6 1.0 C2A A:HEM150 4.4 33.5 1.0

R.J.Radford, P.C.Nguyen, T.B.Ditri, J.S.Figueroa, F.A.Tezcan. Controlled Protein Dimerization Through Hybrid Coordination Motifs. Inorg.Chem. V. 49 4362 2010.
ISSN: ISSN 0020-1669
PubMed: 20377257
DOI: 10.1021/IC100534Y