Iron in PDB 5ufj: Crystal Structure of Carbonmonoxy Hemoglobin S (Liganded Sickle Cell Hemoglobin) Complexed with Gbt Compound 6

The structure of Crystal Structure of Carbonmonoxy Hemoglobin S (Liganded Sickle Cell Hemoglobin) Complexed with Gbt Compound 6, PDB code: 5ufj was solved by J.R.Partridge, R.M.Choy, Z.Li, B.Metcalf, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.76 / 2.05
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.411, 58.881, 174.386, 90.00, 90.00, 90.00
R / Rfree (%)	21.1 / 25.4

The binding sites of Iron atom in the Crystal Structure of Carbonmonoxy Hemoglobin S (Liganded Sickle Cell Hemoglobin) Complexed with Gbt Compound 6 (pdb code 5ufj). 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 Gbt Compound 6, PDB code: 5ufj:
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 Gbt Compound 6


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 Gbt Compound 6 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:68.5 occ:1.00 FE A:HEM201 0.0 68.5 1.0 ND A:HEM201 1.9 75.1 1.0 C A:CMO202 2.0 0.5 1.0 NA A:HEM201 2.0 71.7 1.0 NB A:HEM201 2.0 58.2 1.0 NC A:HEM201 2.1 58.5 1.0 NE2 A:HIS87 2.3 83.8 1.0 C4D A:HEM201 2.9 81.0 1.0 C1D A:HEM201 2.9 80.6 1.0 C1A A:HEM201 3.0 78.4 1.0 C4C A:HEM201 3.1 60.0 1.0 C1B A:HEM201 3.1 67.1 1.0 C4B A:HEM201 3.1 53.5 1.0 O A:CMO202 3.1 0.4 1.0 C4A A:HEM201 3.1 72.9 1.0 C1C A:HEM201 3.1 53.7 1.0 CE1 A:HIS87 3.2 82.9 1.0 CD2 A:HIS87 3.3 68.7 1.0 CHA A:HEM201 3.3 80.3 1.0 CHD A:HEM201 3.4 64.8 1.0 CHB A:HEM201 3.5 81.0 1.0 CHC A:HEM201 3.5 52.2 1.0 C3D A:HEM201 4.1 78.3 1.0 C2D A:HEM201 4.1 74.8 1.0 C2A A:HEM201 4.2 78.9 1.0 C3B A:HEM201 4.3 55.6 1.0 C2B A:HEM201 4.3 66.4 1.0 C3A A:HEM201 4.3 81.9 1.0 C3C A:HEM201 4.3 56.1 1.0 ND1 A:HIS87 4.3 80.2 1.0 C2C A:HEM201 4.4 52.2 1.0 CG A:HIS87 4.4 72.5 1.0 NE2 A:HIS58 4.4 0.2 1.0 CE1 A:HIS58 4.6 0.1 1.0

Iron binding site 2 out of 4 in the Crystal Structure of Carbonmonoxy Hemoglobin S (Liganded Sickle Cell Hemoglobin) Complexed with Gbt Compound 6


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 Gbt Compound 6 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:64.0 occ:1.00 FE B:HEM201 0.0 64.0 1.0 C B:CMO202 1.6 0.8 1.0 NC B:HEM201 2.0 70.7 1.0 ND B:HEM201 2.0 74.0 1.0 NA B:HEM201 2.0 79.4 1.0 NB B:HEM201 2.2 78.1 1.0 NE2 B:HIS92 2.5 63.3 1.0 O B:CMO202 2.6 0.2 1.0 C4C B:HEM201 3.0 66.5 1.0 C4D B:HEM201 3.0 82.5 1.0 C1D B:HEM201 3.0 72.9 1.0 C1A B:HEM201 3.0 81.3 1.0 C1C B:HEM201 3.1 67.1 1.0 C4A B:HEM201 3.1 86.9 1.0 C1B B:HEM201 3.2 79.6 1.0 CD2 B:HIS92 3.2 68.2 1.0 C4B B:HEM201 3.2 74.2 1.0 CHD B:HEM201 3.4 74.1 1.0 CHA B:HEM201 3.4 82.5 1.0 CHB B:HEM201 3.5 86.2 1.0 CHC B:HEM201 3.5 66.8 1.0 CE1 B:HIS92 3.6 77.5 1.0 C3C B:HEM201 4.2 65.4 1.0 C3D B:HEM201 4.2 88.3 1.0 C2C B:HEM201 4.2 68.1 1.0 C2D B:HEM201 4.2 78.7 1.0 C2A B:HEM201 4.3 85.7 1.0 NE2 B:HIS63 4.3 88.4 1.0 C3A B:HEM201 4.3 83.4 1.0 C2B B:HEM201 4.4 82.0 1.0 C3B B:HEM201 4.4 75.9 1.0 CG B:HIS92 4.4 78.0 1.0 ND1 B:HIS92 4.6 82.6 1.0 CE1 B:HIS63 4.7 94.7 1.0 CG2 B:VAL67 4.9 72.3 1.0

Iron binding site 3 out of 4 in the Crystal Structure of Carbonmonoxy Hemoglobin S (Liganded Sickle Cell Hemoglobin) Complexed with Gbt Compound 6


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 Gbt Compound 6 within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:35.4 occ:1.00 FE C:HEM201 0.0 35.4 1.0 C C:CMO202 1.8 0.1 1.0 ND C:HEM201 2.0 45.9 1.0 NB C:HEM201 2.0 34.0 1.0 NC C:HEM201 2.0 33.2 1.0 NA C:HEM201 2.1 38.1 1.0 NE2 C:HIS87 2.2 33.6 1.0 C1D C:HEM201 2.9 39.6 1.0 C4C C:HEM201 3.0 35.0 1.0 C4A C:HEM201 3.0 41.0 1.0 C1B C:HEM201 3.0 34.7 1.0 O C:CMO202 3.0 0.7 1.0 C4D C:HEM201 3.1 50.7 1.0 CE1 C:HIS87 3.1 42.8 1.0 C4B C:HEM201 3.1 40.2 1.0 C1C C:HEM201 3.1 35.3 1.0 C1A C:HEM201 3.1 53.2 1.0 CD2 C:HIS87 3.2 42.5 1.0 CHD C:HEM201 3.3 37.1 1.0 CHB C:HEM201 3.3 35.4 1.0 CHC C:HEM201 3.5 41.4 1.0 CHA C:HEM201 3.5 46.5 1.0 C2D C:HEM201 4.2 44.3 1.0 C3C C:HEM201 4.2 41.2 1.0 ND1 C:HIS87 4.2 35.1 1.0 C3D C:HEM201 4.2 55.8 1.0 NE2 C:HIS58 4.2 60.1 1.0 C3A C:HEM201 4.2 41.5 1.0 C2B C:HEM201 4.2 35.8 1.0 C3B C:HEM201 4.3 31.3 1.0 C2C C:HEM201 4.3 36.0 1.0 CG C:HIS87 4.3 40.5 1.0 C2A C:HEM201 4.3 42.3 1.0 CE1 C:HIS58 4.6 47.3 1.0 CG2 C:VAL62 4.8 39.6 1.0

Iron binding site 4 out of 4 in the Crystal Structure of Carbonmonoxy Hemoglobin S (Liganded Sickle Cell Hemoglobin) Complexed with Gbt Compound 6


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 Gbt Compound 6 within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe201 b:90.3 occ:1.00 FE D:HEM201 0.0 90.3 1.0 C D:CMO202 1.9 0.3 1.0 NB D:HEM201 2.0 87.2 1.0 ND D:HEM201 2.0 94.4 1.0 NC D:HEM201 2.0 80.9 1.0 NA D:HEM201 2.1 0.8 1.0 NE2 D:HIS92 2.4 93.8 1.0 C4B D:HEM201 3.0 80.5 1.0 O D:CMO202 3.0 0.4 1.0 C1C D:HEM201 3.0 75.4 1.0 C4D D:HEM201 3.0 0.0 1.0 C1A D:HEM201 3.1 0.4 1.0 C4C D:HEM201 3.1 79.5 1.0 CE1 D:HIS92 3.1 93.2 1.0 C1D D:HEM201 3.1 91.2 1.0 C1B D:HEM201 3.1 91.4 1.0 C4A D:HEM201 3.1 0.2 1.0 CD2 D:HIS92 3.3 92.8 1.0 CHC D:HEM201 3.3 75.3 1.0 CHA D:HEM201 3.4 0.8 1.0 CHD D:HEM201 3.5 84.2 1.0 CHB D:HEM201 3.5 98.9 1.0 ND1 D:HIS92 4.1 96.7 1.0 C3B D:HEM201 4.2 80.7 1.0 C2C D:HEM201 4.2 72.1 1.0 CG D:HIS92 4.2 92.8 1.0 C3D D:HEM201 4.2 0.5 1.0 C3C D:HEM201 4.3 73.0 1.0 C2B D:HEM201 4.3 87.1 1.0 C2D D:HEM201 4.3 97.0 1.0 C2A D:HEM201 4.3 0.4 1.0 C3A D:HEM201 4.3 0.8 1.0 CE1 D:HIS63 4.4 0.9 1.0 NE2 D:HIS63 4.4 0.4 1.0

B.Metcalf, C.Chuang, K.Dufu, M.P.Patel, A.Silva-Garcia, C.Johnson, Q.Lu, J.R.Partridge, L.Patskovska, Y.Patskovsky, S.C.Almo, M.P.Jacobson, L.Hua, Q.Xu, S.L.Gwaltney, C.Yee, J.Harris, B.P.Morgan, J.James, D.Xu, A.Hutchaleelaha, K.Paulvannan, D.Oksenberg, Z.Li. Discovery of GBT440, An Orally Bioavailable R-State Stabilizer of Sickle Cell Hemoglobin. Acs Med Chem Lett V. 8 321 2017.
ISSN: ISSN 1948-5875
PubMed: 28337324
DOI: 10.1021/ACSMEDCHEMLETT.6B00491