Iron in PDB 2vhb: Azide Adduct of the Bacterial Hemoglobin From Vitreoscilla Stercoraria

The structure of Azide Adduct of the Bacterial Hemoglobin From Vitreoscilla Stercoraria, PDB code: 2vhb was solved by C.Tarricone, A.Galizzi, A.Coda, P.Ascenzi, M.Bolognesi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 1.76
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	62.720, 40.190, 62.940, 90.00, 106.55, 90.00
R / Rfree (%)	19.7 / n/a

The binding sites of Iron atom in the Azide Adduct of the Bacterial Hemoglobin From Vitreoscilla Stercoraria (pdb code 2vhb). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Azide Adduct of the Bacterial Hemoglobin From Vitreoscilla Stercoraria, PDB code: 2vhb:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Azide Adduct of the Bacterial Hemoglobin From Vitreoscilla Stercoraria


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Azide Adduct of the Bacterial Hemoglobin From Vitreoscilla Stercoraria within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe150 b:14.8 occ:1.00 FE A:HEM150 0.0 14.8 1.0 ND A:HEM150 1.8 7.8 1.0 NB A:HEM150 1.9 13.2 1.0 NA A:HEM150 2.0 19.1 1.0 NE2 A:HIS85 2.0 11.7 1.0 NC A:HEM150 2.0 11.7 1.0 N1 A:AZI170 2.0 24.4 1.0 N2 A:AZI170 2.7 49.1 1.0 CE1 A:HIS85 2.9 11.0 1.0 C1D A:HEM150 2.9 13.8 1.0 C4D A:HEM150 3.0 7.8 1.0 C4B A:HEM150 3.0 20.6 1.0 C1B A:HEM150 3.0 11.1 1.0 C4A A:HEM150 3.0 12.6 1.0 C4C A:HEM150 3.0 17.4 1.0 C1C A:HEM150 3.0 10.2 1.0 C1A A:HEM150 3.0 26.4 1.0 CD2 A:HIS85 3.0 9.9 1.0 CHB A:HEM150 3.3 8.3 1.0 CHD A:HEM150 3.4 14.9 1.0 CHA A:HEM150 3.4 21.7 1.0 CHC A:HEM150 3.4 14.9 1.0 N3 A:AZI170 3.6 25.9 1.0 ND1 A:HIS85 4.0 15.0 1.0 O A:HOH201 4.0 22.1 1.0 CG A:HIS85 4.1 13.8 1.0 C2D A:HEM150 4.1 21.5 1.0 C3D A:HEM150 4.2 13.2 1.0 C3B A:HEM150 4.2 13.0 1.0 C2B A:HEM150 4.2 18.6 1.0 C3A A:HEM150 4.2 20.2 1.0 C2C A:HEM150 4.2 10.0 1.0 C3C A:HEM150 4.3 9.9 1.0 C2A A:HEM150 4.3 21.2 1.0 CD2 A:LEU57 4.5 29.4 1.0 CG2 A:ILE81 5.0 16.5 1.0

Iron binding site 2 out of 2 in the Azide Adduct of the Bacterial Hemoglobin From Vitreoscilla Stercoraria


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Azide Adduct of the Bacterial Hemoglobin From Vitreoscilla Stercoraria within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe150 b:13.9 occ:1.00 FE B:HEM150 0.0 13.9 1.0 N1 B:AZI160 1.9 23.0 1.0 ND B:HEM150 1.9 11.9 1.0 NB B:HEM150 2.0 12.9 1.0 NC B:HEM150 2.0 9.5 1.0 NE2 B:HIS85 2.0 9.7 1.0 NA B:HEM150 2.0 22.8 1.0 N2 B:AZI160 2.7 36.7 1.0 CE1 B:HIS85 2.9 13.1 1.0 C1D B:HEM150 2.9 16.2 1.0 C4C B:HEM150 3.0 17.9 1.0 C4D B:HEM150 3.0 18.1 1.0 C1C B:HEM150 3.0 12.4 1.0 C1B B:HEM150 3.0 15.1 1.0 C4B B:HEM150 3.0 15.5 1.0 C1A B:HEM150 3.1 18.7 1.0 C4A B:HEM150 3.1 21.8 1.0 CD2 B:HIS85 3.1 8.6 1.0 CHD B:HEM150 3.3 15.8 1.0 CHA B:HEM150 3.4 23.1 1.0 CHB B:HEM150 3.4 15.2 1.0 CHC B:HEM150 3.4 15.6 1.0 N3 B:AZI160 3.7 34.0 1.0 ND1 B:HIS85 4.0 13.6 1.0 O B:HOH200 4.1 15.1 1.0 CG B:HIS85 4.2 13.6 1.0 C2D B:HEM150 4.2 21.3 1.0 C3C B:HEM150 4.2 16.0 1.0 C3D B:HEM150 4.2 25.4 1.0 C2C B:HEM150 4.2 18.0 1.0 C3B B:HEM150 4.3 12.1 1.0 C2B B:HEM150 4.3 10.7 1.0 C2A B:HEM150 4.3 15.3 1.0 C3A B:HEM150 4.3 14.7 1.0 CD2 B:LEU57 4.7 39.2 1.0 CG2 B:ILE81 4.9 17.0 1.0

C.Tarricone, A.Galizzi, A.Coda, P.Ascenzi, M.Bolognesi. Unusual Structure of the Oxygen-Binding Site in the Dimeric Bacterial Hemoglobin From Vitreoscilla Sp. Structure V. 5 497 1997.
ISSN: ISSN 0969-2126
PubMed: 9115439
DOI: 10.1016/S0969-2126(97)00206-2