Iron in PDB 3wfw: Crystal Structure of the Closed Form of the Hgbrl'S Globin Domain

The structure of Crystal Structure of the Closed Form of the Hgbrl'S Globin Domain, PDB code: 3wfw was solved by A.H.Teh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.51 / 1.65
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	67.240, 54.400, 44.710, 90.00, 106.17, 90.00
R / Rfree (%)	15.1 / 16.9

The binding sites of Iron atom in the Crystal Structure of the Closed Form of the Hgbrl'S Globin Domain (pdb code 3wfw). 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 the Closed Form of the Hgbrl'S Globin Domain, PDB code: 3wfw:

Iron binding site 1 out of 1 in the Crystal Structure of the Closed Form of the Hgbrl'S Globin Domain


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 Closed Form of the Hgbrl'S Globin Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:12.7 occ:1.00 FE A:HEM201 0.0 12.7 1.0 NA A:HEM201 2.0 9.6 1.0 NB A:HEM201 2.0 12.3 1.0 ND A:HEM201 2.0 9.1 1.0 NC A:HEM201 2.0 11.9 1.0 NE2 A:HIS81 2.1 13.8 1.0 C4A A:HEM201 3.0 13.3 1.0 C4D A:HEM201 3.0 11.0 1.0 C1A A:HEM201 3.0 13.0 1.0 C1B A:HEM201 3.0 10.5 1.0 C1C A:HEM201 3.1 12.0 1.0 C4B A:HEM201 3.1 11.7 1.0 C1D A:HEM201 3.1 11.0 1.0 CD2 A:HIS81 3.1 11.5 1.0 CE1 A:HIS81 3.1 12.4 1.0 C4C A:HEM201 3.1 11.5 1.0 CHB A:HEM201 3.4 11.0 1.0 CHA A:HEM201 3.4 11.7 1.0 CHC A:HEM201 3.4 11.2 1.0 CHD A:HEM201 3.5 11.5 1.0 ND1 A:HIS81 4.2 11.8 1.0 C3A A:HEM201 4.2 12.1 1.0 CG A:HIS81 4.2 11.2 1.0 C2A A:HEM201 4.2 13.9 1.0 C3D A:HEM201 4.3 17.1 1.0 C2B A:HEM201 4.3 12.5 1.0 C3B A:HEM201 4.3 10.3 1.0 C2C A:HEM201 4.3 11.2 1.0 C2D A:HEM201 4.3 14.8 1.0 C3C A:HEM201 4.3 13.4 1.0

A.H.Teh, J.A.Saito, N.Najimudin, M.Alam. Crystal Structure of A Novel Site-Swapped Globin: Proximal and Distal Sites Constituted By Two Separate Subunits To Be Published.