Iron in PDB 1s61: Crystal Structure of "Truncated" Hemoglobin N (Hbn) From Mycobacterium Tuberculosis, Soaked with Butyl-Isocyanide

The structure of Crystal Structure of "Truncated" Hemoglobin N (Hbn) From Mycobacterium Tuberculosis, Soaked with Butyl-Isocyanide, PDB code: 1s61 was solved by M.Milani, A.Pesce, Y.Ouellet, S.Dewilde, J.Friedman, P.Ascenzi, M.Guertin, M.Bolognesi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	43.534, 61.432, 91.785, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 25.1

The structure of Crystal Structure of "Truncated" Hemoglobin N (Hbn) From Mycobacterium Tuberculosis, Soaked with Butyl-Isocyanide also contains other interesting chemical elements:

Potassium

(K)

1 atom

The binding sites of Iron atom in the Crystal Structure of "Truncated" Hemoglobin N (Hbn) From Mycobacterium Tuberculosis, Soaked with Butyl-Isocyanide (pdb code 1s61). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of "Truncated" Hemoglobin N (Hbn) From Mycobacterium Tuberculosis, Soaked with Butyl-Isocyanide, PDB code: 1s61:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of "Truncated" Hemoglobin N (Hbn) From Mycobacterium Tuberculosis, Soaked with Butyl-Isocyanide


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 "Truncated" Hemoglobin N (Hbn) From Mycobacterium Tuberculosis, Soaked with Butyl-Isocyanide within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe144 b:20.6 occ:1.00 FE A:HEC144 0.0 20.6 1.0 C A:CYN245 1.9 24.3 1.0 NE2 A:HIS81 1.9 22.5 1.0 NB A:HEC144 2.0 21.5 1.0 NA A:HEC144 2.0 22.4 1.0 ND A:HEC144 2.0 21.1 1.0 NC A:HEC144 2.1 22.0 1.0 CE1 A:HIS81 2.8 24.7 1.0 C1B A:HEC144 3.0 21.3 1.0 C4B A:HEC144 3.0 21.6 1.0 C1A A:HEC144 3.0 23.6 1.0 C4D A:HEC144 3.0 21.8 1.0 C4A A:HEC144 3.0 21.6 1.0 N A:CYN245 3.0 24.9 1.0 CD2 A:HIS81 3.1 21.6 1.0 C4C A:HEC144 3.1 22.9 1.0 C1C A:HEC144 3.1 21.0 1.0 C1D A:HEC144 3.1 21.7 1.0 CHA A:HEC144 3.4 24.1 1.0 CHB A:HEC144 3.4 24.1 1.0 CHC A:HEC144 3.4 21.7 1.0 CHD A:HEC144 3.5 21.2 1.0 ND1 A:HIS81 4.0 23.5 1.0 CG A:HIS81 4.1 24.2 1.0 C2B A:HEC144 4.2 21.1 1.0 C3B A:HEC144 4.2 22.1 1.0 C3A A:HEC144 4.2 21.9 1.0 C2A A:HEC144 4.2 23.1 1.0 C3D A:HEC144 4.3 23.4 1.0 C3C A:HEC144 4.3 22.8 1.0 C2C A:HEC144 4.3 21.5 1.0 C2D A:HEC144 4.3 22.0 1.0 NE2 A:GLN58 4.8 25.2 1.0

Iron binding site 2 out of 2 in the Crystal Structure of "Truncated" Hemoglobin N (Hbn) From Mycobacterium Tuberculosis, Soaked with Butyl-Isocyanide


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 "Truncated" Hemoglobin N (Hbn) From Mycobacterium Tuberculosis, Soaked with Butyl-Isocyanide within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe144 b:21.5 occ:0.50 FE B:HEM144 0.0 21.5 0.5 C B:CYN345 1.7 21.6 1.0 NB B:HEM144 2.0 23.3 0.5 NC B:HEM144 2.0 23.3 0.5 NA B:HEM144 2.1 21.1 0.5 ND B:HEM144 2.1 24.0 0.5 NE2 B:HIS81 2.1 22.6 1.0 N B:CYN345 2.8 21.5 1.0 C4B B:HEM144 3.0 25.4 0.5 C1C B:HEM144 3.0 23.3 0.5 C4A B:HEM144 3.0 20.9 0.5 C1B B:HEM144 3.0 23.7 0.5 C4C B:HEM144 3.0 24.6 0.5 CE1 B:HIS81 3.1 24.3 1.0 C4D B:HEM144 3.1 24.4 0.5 C1D B:HEM144 3.1 22.3 0.5 CD2 B:HIS81 3.1 24.4 1.0 C1A B:HEM144 3.1 23.8 0.5 CHB B:HEM144 3.4 23.3 0.5 CHC B:HEM144 3.4 23.9 0.5 CHD B:HEM144 3.4 24.0 0.5 CHA B:HEM144 3.5 24.8 0.5 ND1 B:HIS81 4.2 25.3 1.0 C3B B:HEM144 4.2 26.5 0.5 C2B B:HEM144 4.2 26.5 0.5 C2C B:HEM144 4.2 25.1 0.5 C3A B:HEM144 4.2 21.3 0.5 CG B:HIS81 4.2 23.6 1.0 C3C B:HEM144 4.3 24.1 0.5 C2A B:HEM144 4.3 22.1 0.5 C3D B:HEM144 4.3 23.4 0.5 C2D B:HEM144 4.3 21.9 0.5 OE1 B:GLN58 5.0 30.2 1.0

M.Milani, A.Pesce, Y.Ouellet, S.Dewilde, J.Friedman, P.Ascenzi, M.Guertin, M.Bolognesi. Heme-Ligand Tunneling in Group I Truncated Hemoglobins J.Biol.Chem. V. 279 21520 2004.
ISSN: ISSN 0021-9258
PubMed: 15016811
DOI: 10.1074/JBC.M401320200