Iron in PDB 3qw1: Crystal Structure of the Zn-RIDC1 Complex Stabilized By Bmh Crosslinks

The structure of Crystal Structure of the Zn-RIDC1 Complex Stabilized By Bmh Crosslinks, PDB code: 3qw1 was solved by E.N.Salgado, F.A.Tezcan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.20 / 2.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	48.298, 61.843, 70.087, 90.00, 102.22, 90.00
R / Rfree (%)	28.8 / 31.8

The structure of Crystal Structure of the Zn-RIDC1 Complex Stabilized By Bmh Crosslinks also contains other interesting chemical elements:

Zinc

(Zn)

5 atoms

The binding sites of Iron atom in the Crystal Structure of the Zn-RIDC1 Complex Stabilized By Bmh Crosslinks (pdb code 3qw1). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of the Zn-RIDC1 Complex Stabilized By Bmh Crosslinks, PDB code: 3qw1:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystal Structure of the Zn-RIDC1 Complex Stabilized By Bmh Crosslinks


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 the Zn-RIDC1 Complex Stabilized By Bmh Crosslinks within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe150 b:36.3 occ:1.00 FE A:HEM150 0.0 36.3 1.0 NC A:HEM150 2.0 35.3 1.0 NE2 A:HIS102 2.0 30.1 1.0 SD A:MET7 2.0 31.8 1.0 NB A:HEM150 2.1 37.2 1.0 NA A:HEM150 2.1 41.4 1.0 ND A:HEM150 2.1 41.7 1.0 CE1 A:HIS102 3.0 30.2 1.0 C1C A:HEM150 3.0 34.3 1.0 C4C A:HEM150 3.0 36.1 1.0 CD2 A:HIS102 3.0 30.5 1.0 C4B A:HEM150 3.1 33.9 1.0 C1B A:HEM150 3.1 37.4 1.0 C1D A:HEM150 3.1 42.2 1.0 C1A A:HEM150 3.1 43.7 1.0 C4A A:HEM150 3.1 42.3 1.0 C4D A:HEM150 3.1 44.9 1.0 CE A:MET7 3.3 30.6 1.0 CG A:MET7 3.3 32.7 1.0 CHC A:HEM150 3.4 34.0 1.0 CHD A:HEM150 3.4 38.8 1.0 CHB A:HEM150 3.5 40.0 1.0 CHA A:HEM150 3.5 44.9 1.0 ND1 A:HIS102 4.1 31.5 1.0 CB A:MET7 4.1 33.1 1.0 CG A:HIS102 4.1 31.5 1.0 C2C A:HEM150 4.2 33.5 1.0 C3C A:HEM150 4.2 34.6 1.0 C3B A:HEM150 4.3 33.7 1.0 C2B A:HEM150 4.3 35.5 1.0 C2D A:HEM150 4.3 46.0 1.0 C2A A:HEM150 4.4 44.5 1.0 C3A A:HEM150 4.4 43.5 1.0 C3D A:HEM150 4.4 47.2 1.0 CA A:MET7 4.9 33.3 1.0

Iron binding site 2 out of 4 in the Crystal Structure of the Zn-RIDC1 Complex Stabilized By Bmh Crosslinks


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of the Zn-RIDC1 Complex Stabilized By Bmh Crosslinks within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe150 b:35.3 occ:1.00 FE B:HEM150 0.0 35.3 1.0 NE2 B:HIS102 1.9 29.8 1.0 NB B:HEM150 1.9 34.5 1.0 NC B:HEM150 2.0 34.0 1.0 ND B:HEM150 2.0 37.5 1.0 NA B:HEM150 2.1 37.8 1.0 SD B:MET7 2.2 32.0 1.0 CD2 B:HIS102 2.9 30.5 1.0 CE1 B:HIS102 2.9 30.1 1.0 C1B B:HEM150 2.9 35.0 1.0 C1D B:HEM150 3.0 38.3 1.0 C4B B:HEM150 3.0 33.0 1.0 C4C B:HEM150 3.0 33.8 1.0 C1C B:HEM150 3.1 32.3 1.0 C4A B:HEM150 3.1 37.9 1.0 C4D B:HEM150 3.1 39.9 1.0 C1A B:HEM150 3.2 39.8 1.0 CHD B:HEM150 3.3 35.7 1.0 CHB B:HEM150 3.3 36.7 1.0 CE B:MET7 3.4 30.5 1.0 CG B:MET7 3.4 32.8 1.0 CHC B:HEM150 3.4 32.0 1.0 CHA B:HEM150 3.5 40.1 1.0 ND1 B:HIS102 4.0 31.5 1.0 CG B:HIS102 4.0 31.7 1.0 C2B B:HEM150 4.2 33.6 1.0 C3B B:HEM150 4.2 32.0 1.0 CB B:MET7 4.2 33.2 1.0 C2D B:HEM150 4.2 40.5 1.0 C3C B:HEM150 4.3 33.3 1.0 C2C B:HEM150 4.3 33.1 1.0 C3D B:HEM150 4.3 41.0 1.0 C3A B:HEM150 4.4 39.0 1.0 C2A B:HEM150 4.4 41.0 1.0

Iron binding site 3 out of 4 in the Crystal Structure of the Zn-RIDC1 Complex Stabilized By Bmh Crosslinks


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of the Zn-RIDC1 Complex Stabilized By Bmh Crosslinks within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe150 b:28.9 occ:1.00 FE C:HEM150 0.0 28.9 1.0 NC C:HEM150 2.0 29.0 1.0 NE2 C:HIS102 2.0 29.4 1.0 SD C:MET7 2.0 31.9 1.0 ND C:HEM150 2.1 32.2 1.0 NB C:HEM150 2.1 29.3 1.0 NA C:HEM150 2.1 32.8 1.0 CE1 C:HIS102 3.0 30.0 1.0 CD2 C:HIS102 3.0 30.1 1.0 C1C C:HEM150 3.0 27.9 1.0 C4C C:HEM150 3.0 30.1 1.0 C1D C:HEM150 3.1 31.5 1.0 C1B C:HEM150 3.1 29.4 1.0 C4A C:HEM150 3.1 34.4 1.0 C4D C:HEM150 3.1 33.7 1.0 C4B C:HEM150 3.1 28.4 1.0 C1A C:HEM150 3.1 36.4 1.0 CE C:MET7 3.1 30.7 1.0 CHD C:HEM150 3.4 31.2 1.0 CHC C:HEM150 3.4 26.9 1.0 CG C:MET7 3.4 32.7 1.0 CHB C:HEM150 3.4 32.5 1.0 CHA C:HEM150 3.5 34.0 1.0 ND1 C:HIS102 4.1 31.5 1.0 CG C:HIS102 4.1 31.5 1.0 CB C:MET7 4.2 33.1 1.0 C2C C:HEM150 4.3 27.5 1.0 C3C C:HEM150 4.3 28.2 1.0 C2B C:HEM150 4.3 29.3 1.0 C2D C:HEM150 4.3 34.2 1.0 C3A C:HEM150 4.3 36.8 1.0 C3D C:HEM150 4.3 35.3 1.0 C2A C:HEM150 4.3 38.4 1.0 C3B C:HEM150 4.3 28.9 1.0 CA C:MET7 5.0 33.3 1.0

Iron binding site 4 out of 4 in the Crystal Structure of the Zn-RIDC1 Complex Stabilized By Bmh Crosslinks


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of the Zn-RIDC1 Complex Stabilized By Bmh Crosslinks within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe150 b:29.2 occ:1.00 FE D:HEM150 0.0 29.2 1.0 NB D:HEM150 1.9 26.9 1.0 ND D:HEM150 2.0 27.4 1.0 NE2 D:HIS102 2.0 29.6 1.0 NC D:HEM150 2.1 26.8 1.0 SD D:MET7 2.1 31.6 1.0 NA D:HEM150 2.1 30.3 1.0 C4B D:HEM150 2.9 26.4 1.0 C1B D:HEM150 2.9 27.7 1.0 C1D D:HEM150 3.0 28.0 1.0 CD2 D:HIS102 3.0 30.2 1.0 CE1 D:HIS102 3.0 30.3 1.0 C4C D:HEM150 3.1 26.5 1.0 C4D D:HEM150 3.1 29.5 1.0 C1C D:HEM150 3.1 25.2 1.0 C4A D:HEM150 3.1 30.0 1.0 C1A D:HEM150 3.2 32.3 1.0 CE D:MET7 3.3 30.4 1.0 CG D:MET7 3.3 32.7 1.0 CHD D:HEM150 3.4 27.2 1.0 CHB D:HEM150 3.4 29.4 1.0 CHC D:HEM150 3.4 25.7 1.0 CHA D:HEM150 3.5 30.3 1.0 C3B D:HEM150 4.1 26.3 1.0 C2B D:HEM150 4.1 27.1 1.0 ND1 D:HIS102 4.1 31.6 1.0 CG D:HIS102 4.2 31.5 1.0 CB D:MET7 4.2 33.2 1.0 C2D D:HEM150 4.2 30.0 1.0 C3D D:HEM150 4.3 30.2 1.0 C3C D:HEM150 4.3 27.0 1.0 C2C D:HEM150 4.3 25.1 1.0 C3A D:HEM150 4.4 31.9 1.0 C2A D:HEM150 4.4 35.0 1.0 CA D:MET7 4.9 33.3 1.0

E.N.Salgado, J.D.Brodin, M.M.To, F.A.Tezcan. Templated Construction of A Zn-Selective Protein Dimerization Motif. Inorg.Chem. V. 50 6323 2011.
ISSN: ISSN 0020-1669
PubMed: 21648390
DOI: 10.1021/IC200746M