Iron in PDB 5e83: Crystal Structure of Carbonmonoxy Hemoglobin S (Liganded Sickle Cell Hemoglobin) Complexed with GBT440, Co-Crystallization Experiment

The structure of Crystal Structure of Carbonmonoxy Hemoglobin S (Liganded Sickle Cell Hemoglobin) Complexed with GBT440, Co-Crystallization Experiment, PDB code: 5e83 was solved by L.Patskovska, Y.Patskovsky, J.B.Bonanno, S.C.Almo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.71 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.777, 59.104, 170.260, 90.00, 90.00, 90.00
R / Rfree (%)	17.7 / 20.8

The binding sites of Iron atom in the Crystal Structure of Carbonmonoxy Hemoglobin S (Liganded Sickle Cell Hemoglobin) Complexed with GBT440, Co-Crystallization Experiment (pdb code 5e83). 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 Carbonmonoxy Hemoglobin S (Liganded Sickle Cell Hemoglobin) Complexed with GBT440, Co-Crystallization Experiment, PDB code: 5e83:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystal Structure of Carbonmonoxy Hemoglobin S (Liganded Sickle Cell Hemoglobin) Complexed with GBT440, Co-Crystallization Experiment


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 Hemoglobin S (Liganded Sickle Cell Hemoglobin) Complexed with GBT440, Co-Crystallization Experiment within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:22.6 occ:1.00 FE A:HEM201 0.0 22.6 1.0 C A:CMO202 1.9 21.2 1.0 ND A:HEM201 1.9 21.7 1.0 NA A:HEM201 2.0 22.9 1.0 NC A:HEM201 2.1 23.2 1.0 NB A:HEM201 2.1 19.6 1.0 NE2 A:HIS87 2.1 23.4 1.0 C1D A:HEM201 2.9 22.1 1.0 C4D A:HEM201 2.9 22.4 1.0 C4B A:HEM201 3.0 20.0 1.0 C4A A:HEM201 3.0 22.7 1.0 C1A A:HEM201 3.0 22.6 1.0 CE1 A:HIS87 3.0 24.9 1.0 C1B A:HEM201 3.1 26.6 1.0 C4C A:HEM201 3.1 20.3 1.0 O A:CMO202 3.1 34.1 1.0 C1C A:HEM201 3.1 20.2 1.0 CD2 A:HIS87 3.1 20.9 1.0 CHD A:HEM201 3.4 22.1 1.0 CHA A:HEM201 3.4 25.8 1.0 CHB A:HEM201 3.4 25.0 1.0 CHC A:HEM201 3.5 19.4 1.0 C2D A:HEM201 4.2 22.7 1.0 ND1 A:HIS87 4.2 23.0 1.0 C3D A:HEM201 4.2 23.5 1.0 C3A A:HEM201 4.2 23.9 1.0 C2A A:HEM201 4.2 26.7 1.0 CG A:HIS87 4.3 22.4 1.0 C2B A:HEM201 4.3 20.7 1.0 C3C A:HEM201 4.3 19.6 1.0 C3B A:HEM201 4.3 20.0 1.0 C2C A:HEM201 4.3 22.3 1.0 NE2 A:HIS58 4.3 28.8 1.0 CG2 A:VAL62 4.8 25.2 1.0

Iron binding site 2 out of 4 in the Crystal Structure of Carbonmonoxy Hemoglobin S (Liganded Sickle Cell Hemoglobin) Complexed with GBT440, Co-Crystallization Experiment


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 Hemoglobin S (Liganded Sickle Cell Hemoglobin) Complexed with GBT440, Co-Crystallization Experiment within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:35.1 occ:1.00 FE B:HEM201 0.0 35.1 1.0 ND B:HEM201 1.9 34.3 1.0 C B:CMO202 1.9 30.9 1.0 NA B:HEM201 2.0 37.0 1.0 NE2 B:HIS92 2.1 35.4 1.0 NC B:HEM201 2.1 37.1 1.0 NB B:HEM201 2.1 36.2 1.0 C4D B:HEM201 2.9 39.1 1.0 C1D B:HEM201 2.9 38.4 1.0 CE1 B:HIS92 3.0 40.0 1.0 C1A B:HEM201 3.0 39.7 1.0 C4A B:HEM201 3.0 37.8 1.0 C4B B:HEM201 3.1 32.5 1.0 O B:CMO202 3.1 40.4 1.0 C1B B:HEM201 3.1 34.7 1.0 C4C B:HEM201 3.1 32.7 1.0 C1C B:HEM201 3.1 32.1 1.0 CD2 B:HIS92 3.2 36.5 1.0 CHA B:HEM201 3.4 39.9 1.0 CHD B:HEM201 3.4 34.4 1.0 CHC B:HEM201 3.4 30.9 1.0 CHB B:HEM201 3.5 39.4 1.0 ND1 B:HIS92 4.1 35.9 1.0 C3D B:HEM201 4.2 40.2 1.0 C2D B:HEM201 4.2 36.5 1.0 C2A B:HEM201 4.2 40.1 1.0 C3A B:HEM201 4.2 41.9 1.0 CG B:HIS92 4.3 34.1 1.0 C2B B:HEM201 4.3 31.6 1.0 C2C B:HEM201 4.3 31.1 1.0 C3C B:HEM201 4.3 31.4 1.0 C3B B:HEM201 4.3 31.5 1.0 NE2 B:HIS63 4.4 41.3 1.0 CG2 B:VAL67 4.8 36.4 1.0

Iron binding site 3 out of 4 in the Crystal Structure of Carbonmonoxy Hemoglobin S (Liganded Sickle Cell Hemoglobin) Complexed with GBT440, Co-Crystallization Experiment


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 Carbonmonoxy Hemoglobin S (Liganded Sickle Cell Hemoglobin) Complexed with GBT440, Co-Crystallization Experiment within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:33.2 occ:1.00 FE C:HEM201 0.0 33.2 1.0 ND C:HEM201 1.9 36.9 1.0 C C:CMO202 1.9 36.5 1.0 NA C:HEM201 2.0 33.6 1.0 NC C:HEM201 2.1 31.7 1.0 NB C:HEM201 2.1 33.1 1.0 NE2 C:HIS87 2.1 30.7 1.0 C4D C:HEM201 2.9 36.0 1.0 C1D C:HEM201 2.9 30.3 1.0 CE1 C:HIS87 3.0 35.6 1.0 C1A C:HEM201 3.0 34.4 1.0 C4A C:HEM201 3.0 31.8 1.0 C4B C:HEM201 3.0 28.6 1.0 O C:CMO202 3.1 32.7 1.0 C4C C:HEM201 3.1 27.8 1.0 C1C C:HEM201 3.1 29.6 1.0 C1B C:HEM201 3.1 31.0 1.0 CD2 C:HIS87 3.2 30.6 1.0 CHA C:HEM201 3.4 37.1 1.0 CHD C:HEM201 3.4 32.4 1.0 CHC C:HEM201 3.4 28.1 1.0 CHB C:HEM201 3.5 30.9 1.0 ND1 C:HIS87 4.1 33.4 1.0 C2D C:HEM201 4.2 38.8 1.0 C3D C:HEM201 4.2 36.4 1.0 C2A C:HEM201 4.2 35.2 1.0 C3A C:HEM201 4.2 36.0 1.0 CG C:HIS87 4.3 31.9 1.0 C2C C:HEM201 4.3 27.7 1.0 C3C C:HEM201 4.3 28.1 1.0 C2B C:HEM201 4.3 28.9 1.0 C3B C:HEM201 4.3 33.7 1.0 NE2 C:HIS58 4.3 42.7 1.0 CG2 C:VAL62 4.8 33.3 1.0

Iron binding site 4 out of 4 in the Crystal Structure of Carbonmonoxy Hemoglobin S (Liganded Sickle Cell Hemoglobin) Complexed with GBT440, Co-Crystallization Experiment


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 Carbonmonoxy Hemoglobin S (Liganded Sickle Cell Hemoglobin) Complexed with GBT440, Co-Crystallization Experiment within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe201 b:33.8 occ:1.00 FE D:HEM201 0.0 33.8 1.0 C D:CMO202 1.9 29.8 1.0 ND D:HEM201 1.9 36.6 1.0 NA D:HEM201 2.0 33.6 1.0 NE2 D:HIS92 2.1 40.3 1.0 NC D:HEM201 2.1 32.3 1.0 NB D:HEM201 2.1 31.9 1.0 C4D D:HEM201 2.9 36.8 1.0 C1D D:HEM201 2.9 33.0 1.0 CE1 D:HIS92 3.0 39.3 1.0 C1A D:HEM201 3.0 44.1 1.0 C4A D:HEM201 3.0 37.7 1.0 C4B D:HEM201 3.1 33.1 1.0 C1B D:HEM201 3.1 33.0 1.0 C4C D:HEM201 3.1 31.8 1.0 O D:CMO202 3.1 37.3 1.0 C1C D:HEM201 3.1 36.0 1.0 CD2 D:HIS92 3.1 31.9 1.0 CHA D:HEM201 3.4 37.3 1.0 CHD D:HEM201 3.4 37.2 1.0 CHC D:HEM201 3.4 30.8 1.0 CHB D:HEM201 3.4 39.8 1.0 ND1 D:HIS92 4.1 37.2 1.0 C2D D:HEM201 4.2 37.6 1.0 C3D D:HEM201 4.2 36.5 1.0 C2A D:HEM201 4.2 39.1 1.0 C3A D:HEM201 4.2 36.8 1.0 CG D:HIS92 4.2 34.8 1.0 C2C D:HEM201 4.3 29.0 1.0 C3C D:HEM201 4.3 34.3 1.0 C2B D:HEM201 4.3 35.6 1.0 C3B D:HEM201 4.3 35.4 1.0 NE2 D:HIS63 4.4 42.9 1.0 CG2 D:VAL67 4.9 35.1 1.0

D.Oksenberg, K.Dufu, M.P.Patel, C.Chuang, Z.Li, Q.Xu, A.Silva-Garcia, C.Zhou, A.Hutchaleelaha, L.Patskovska, Y.Patskovsky, S.C.Almo, U.Sinha, B.W.Metcalf, D.R.Archer. GBT440 Increases Haemoglobin Oxygen Affinity, Reduces Sickling and Prolongs Rbc Half-Life in A Murine Model of Sickle Cell Disease. Br.J.Haematol. V. 175 141 2016.
ISSN: ISSN 0007-1048
PubMed: 27378309
DOI: 10.1111/BJH.14214