Iron in PDB 5e6e: Crystal Structure of Carbonmonoxy Sickle Hemoglobin in R-State Conformation

The structure of Crystal Structure of Carbonmonoxy Sickle Hemoglobin in R-State Conformation, PDB code: 5e6e was solved by M.K.Safo, M.H.Ahmed, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.61 / 1.76
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	53.352, 53.352, 191.068, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 24.3

The binding sites of Iron atom in the Crystal Structure of Carbonmonoxy Sickle Hemoglobin in R-State Conformation (pdb code 5e6e). 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 Carbonmonoxy Sickle Hemoglobin in R-State Conformation, PDB code: 5e6e:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Carbonmonoxy Sickle Hemoglobin in R-State Conformation


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 Carbonmonoxy Sickle Hemoglobin in R-State Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe202 b:17.0 occ:1.00 FE A:HEM202 0.0 17.0 1.0 C A:CMO201 1.9 12.4 1.0 NC A:HEM202 2.0 13.7 1.0 NA A:HEM202 2.0 15.4 1.0 ND A:HEM202 2.0 14.9 1.0 NB A:HEM202 2.0 14.8 1.0 NE2 A:HIS87 2.1 16.4 1.0 C1C A:HEM202 3.0 13.3 1.0 C1B A:HEM202 3.0 18.6 1.0 C4A A:HEM202 3.0 15.1 1.0 C4C A:HEM202 3.0 13.9 1.0 CE1 A:HIS87 3.1 12.6 1.0 C1A A:HEM202 3.1 14.4 1.0 C1D A:HEM202 3.1 17.4 1.0 O A:CMO201 3.1 16.7 1.0 C4D A:HEM202 3.1 20.0 1.0 C4B A:HEM202 3.1 12.5 1.0 CD2 A:HIS87 3.1 19.9 1.0 CHB A:HEM202 3.4 14.7 1.0 CHD A:HEM202 3.4 15.8 1.0 CHC A:HEM202 3.5 11.6 1.0 CHA A:HEM202 3.5 15.7 1.0 ND1 A:HIS87 4.2 15.9 1.0 CG A:HIS87 4.3 17.6 1.0 C2C A:HEM202 4.3 11.6 1.0 C3A A:HEM202 4.3 18.5 1.0 C2B A:HEM202 4.3 12.2 1.0 C3C A:HEM202 4.3 14.6 1.0 C2A A:HEM202 4.3 16.6 1.0 C2D A:HEM202 4.3 17.5 1.0 C3D A:HEM202 4.3 19.3 1.0 C3B A:HEM202 4.3 13.6 1.0 NE2 A:HIS58 4.4 19.1 1.0 CG2 A:VAL62 5.0 15.2 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Carbonmonoxy Sickle Hemoglobin in R-State Conformation


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 Carbonmonoxy Sickle Hemoglobin in R-State Conformation within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe202 b:23.1 occ:1.00 FE B:HEM202 0.0 23.1 1.0 C B:CMO201 1.8 18.6 1.0 ND B:HEM202 2.0 22.9 1.0 NB B:HEM202 2.0 23.9 1.0 NC B:HEM202 2.1 20.1 1.0 NA B:HEM202 2.1 19.8 1.0 NE2 B:HIS92 2.1 20.9 1.0 O B:CMO201 3.0 17.0 1.0 CE1 B:HIS92 3.1 21.3 1.0 C1A B:HEM202 3.1 25.4 1.0 C4D B:HEM202 3.1 22.0 1.0 C1C B:HEM202 3.1 25.3 1.0 C4B B:HEM202 3.1 25.3 1.0 C1D B:HEM202 3.1 23.9 1.0 C4A B:HEM202 3.1 25.9 1.0 C4C B:HEM202 3.1 23.3 1.0 C1B B:HEM202 3.1 22.0 1.0 CD2 B:HIS92 3.1 21.7 1.0 CHA B:HEM202 3.4 23.4 1.0 CHC B:HEM202 3.4 23.4 1.0 CHD B:HEM202 3.5 20.2 1.0 CHB B:HEM202 3.5 21.6 1.0 ND1 B:HIS92 4.2 25.2 1.0 CG B:HIS92 4.3 21.2 1.0 C3D B:HEM202 4.3 28.1 1.0 C2C B:HEM202 4.3 18.0 1.0 C2D B:HEM202 4.3 27.5 1.0 C2A B:HEM202 4.3 25.1 1.0 C3A B:HEM202 4.3 23.6 1.0 C3C B:HEM202 4.4 22.2 1.0 C2B B:HEM202 4.4 22.9 1.0 C3B B:HEM202 4.4 25.6 1.0 NE2 B:HIS63 4.5 27.2 1.0 CG2 B:VAL67 4.6 26.0 1.0

M.S.Ghatge, M.H.Ahmed, A.S.Omar, P.P.Pagare, S.Rosef, G.E.Kellogg, O.Abdulmalik, M.K.Safo. Crystal Structure of Carbonmonoxy Sickle Hemoglobin in R-State Conformation. J.Struct.Biol. V. 194 446 2016.
ISSN: ESSN 1095-8657
PubMed: 27085422
DOI: 10.1016/J.JSB.2016.04.003