Iron in PDB 5u3i: Crystal Structure of Carbonmonoxy Hemoglobin S (Liganded Sickle Cell Hemoglobin) Complexed with Gbt Compound 31

The structure of Crystal Structure of Carbonmonoxy Hemoglobin S (Liganded Sickle Cell Hemoglobin) Complexed with Gbt Compound 31, PDB code: 5u3i 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)	29.81 / 1.95
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	57.385, 59.040, 172.637, 90.00, 90.00, 90.00
R / Rfree (%)	20.6 / 25.3

The binding sites of Iron atom in the Crystal Structure of Carbonmonoxy Hemoglobin S (Liganded Sickle Cell Hemoglobin) Complexed with Gbt Compound 31 (pdb code 5u3i). 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 31, PDB code: 5u3i:
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 31


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 31 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:83.8 occ:1.00 FE A:HEM201 0.0 83.8 1.0 C A:CMO202 1.8 0.4 1.0 ND A:HEM201 1.9 88.2 1.0 NC A:HEM201 1.9 69.3 1.0 NB A:HEM201 2.0 71.0 1.0 NA A:HEM201 2.1 90.8 1.0 NE2 A:HIS87 2.3 0.4 1.0 O A:CMO202 2.8 0.0 1.0 C4D A:HEM201 2.9 88.5 1.0 C1D A:HEM201 3.0 90.0 1.0 C1C A:HEM201 3.0 63.7 1.0 C4C A:HEM201 3.0 70.0 1.0 CE1 A:HIS87 3.0 0.1 1.0 C4B A:HEM201 3.0 69.8 1.0 C1A A:HEM201 3.0 90.4 1.0 C1B A:HEM201 3.1 84.2 1.0 C4A A:HEM201 3.2 84.5 1.0 CHA A:HEM201 3.3 92.6 1.0 CHC A:HEM201 3.4 61.7 1.0 CHD A:HEM201 3.4 75.2 1.0 CD2 A:HIS87 3.4 94.8 1.0 CHB A:HEM201 3.6 79.6 1.0 C3D A:HEM201 4.1 91.8 1.0 C2D A:HEM201 4.1 87.0 1.0 C2C A:HEM201 4.2 63.0 1.0 ND1 A:HIS87 4.2 0.5 1.0 C3C A:HEM201 4.2 65.8 1.0 C3B A:HEM201 4.3 70.6 1.0 C2A A:HEM201 4.3 95.3 1.0 C2B A:HEM201 4.3 73.5 1.0 C3A A:HEM201 4.3 94.3 1.0 CG A:HIS87 4.4 96.8 1.0 CE1 A:HIS58 4.6 0.1 1.0 NE2 A:HIS58 4.6 0.5 1.0 CG2 A:VAL62 4.9 79.6 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 31


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 31 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:61.6 occ:1.00 FE B:HEM201 0.0 61.6 1.0 C B:CMO202 2.0 0.4 1.0 ND B:HEM201 2.0 73.3 1.0 NA B:HEM201 2.0 73.0 1.0 NC B:HEM201 2.0 59.3 1.0 NB B:HEM201 2.1 61.0 1.0 NE2 B:HIS92 2.3 76.0 1.0 O B:CMO202 2.9 0.4 1.0 C1D B:HEM201 3.0 66.8 1.0 C4C B:HEM201 3.0 60.2 1.0 C4A B:HEM201 3.0 80.8 1.0 C4D B:HEM201 3.0 76.0 1.0 C1A B:HEM201 3.1 79.3 1.0 C1C B:HEM201 3.1 60.3 1.0 C1B B:HEM201 3.1 66.9 1.0 C4B B:HEM201 3.1 58.3 1.0 CD2 B:HIS92 3.1 72.3 1.0 CHD B:HEM201 3.4 59.8 1.0 CE1 B:HIS92 3.4 83.9 1.0 CHB B:HEM201 3.4 76.5 1.0 CHA B:HEM201 3.4 80.6 1.0 CHC B:HEM201 3.5 60.6 1.0 C2D B:HEM201 4.2 75.1 1.0 C3C B:HEM201 4.2 59.4 1.0 C3D B:HEM201 4.2 76.3 1.0 C3A B:HEM201 4.2 80.5 1.0 C2A B:HEM201 4.3 77.3 1.0 C2C B:HEM201 4.3 60.8 1.0 C2B B:HEM201 4.3 66.4 1.0 C3B B:HEM201 4.3 62.7 1.0 CG B:HIS92 4.4 76.7 1.0 ND1 B:HIS92 4.4 86.2 1.0 NE2 B:HIS63 4.5 85.0 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 31


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 31 within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:44.7 occ:1.00 FE C:HEM201 0.0 44.7 1.0 C C:CMO202 1.7 0.3 1.0 ND C:HEM201 2.0 50.3 1.0 NC C:HEM201 2.0 39.9 1.0 NB C:HEM201 2.1 39.4 1.0 NA C:HEM201 2.1 45.2 1.0 NE2 C:HIS87 2.3 47.7 1.0 O C:CMO202 2.7 0.5 1.0 C1D C:HEM201 3.0 50.2 1.0 C4C C:HEM201 3.0 44.2 1.0 C4A C:HEM201 3.0 52.6 1.0 C1B C:HEM201 3.1 43.8 1.0 C4D C:HEM201 3.1 56.1 1.0 C1C C:HEM201 3.1 39.1 1.0 C1A C:HEM201 3.1 53.4 1.0 C4B C:HEM201 3.1 43.2 1.0 CD2 C:HIS87 3.1 44.1 1.0 CE1 C:HIS87 3.3 50.1 1.0 CHD C:HEM201 3.4 40.4 1.0 CHB C:HEM201 3.4 46.1 1.0 CHA C:HEM201 3.5 55.6 1.0 CHC C:HEM201 3.5 44.8 1.0 C2D C:HEM201 4.2 50.7 1.0 C3D C:HEM201 4.3 57.6 1.0 C3C C:HEM201 4.3 42.4 1.0 C2C C:HEM201 4.3 35.9 1.0 C3A C:HEM201 4.3 47.3 1.0 C2A C:HEM201 4.3 59.2 1.0 C2B C:HEM201 4.3 44.9 1.0 C3B C:HEM201 4.3 37.5 1.0 CG C:HIS87 4.3 48.9 1.0 NE2 C:HIS58 4.4 66.4 1.0 ND1 C:HIS87 4.4 49.7 1.0 CE1 C:HIS58 4.6 77.1 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 31


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 31 within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe201 b:87.4 occ:1.00 FE D:HEM201 0.0 87.4 1.0 C D:CMO202 1.5 0.5 1.0 ND D:HEM201 2.0 98.4 1.0 NC D:HEM201 2.0 92.9 1.0 NA D:HEM201 2.0 0.8 1.0 NB D:HEM201 2.1 86.9 1.0 NE2 D:HIS92 2.4 91.4 1.0 O D:CMO202 2.6 0.1 1.0 C4C D:HEM201 3.0 90.5 1.0 C1D D:HEM201 3.0 98.2 1.0 C4D D:HEM201 3.0 97.6 1.0 C1A D:HEM201 3.0 1.0 1.0 C1C D:HEM201 3.1 85.2 1.0 C4A D:HEM201 3.1 0.1 1.0 C1B D:HEM201 3.1 85.4 1.0 C4B D:HEM201 3.1 78.6 1.0 CD2 D:HIS92 3.2 89.1 1.0 CHD D:HEM201 3.4 95.9 1.0 CHA D:HEM201 3.4 0.6 1.0 CHB D:HEM201 3.5 94.5 1.0 CHC D:HEM201 3.5 76.4 1.0 CE1 D:HIS92 3.5 96.1 1.0 C3C D:HEM201 4.2 83.2 1.0 C2D D:HEM201 4.2 98.2 1.0 C3D D:HEM201 4.2 0.7 1.0 C2C D:HEM201 4.3 79.8 1.0 C2A D:HEM201 4.3 0.0 1.0 C3A D:HEM201 4.3 0.5 1.0 C2B D:HEM201 4.3 82.8 1.0 C3B D:HEM201 4.3 78.9 1.0 CG D:HIS92 4.4 90.4 1.0 ND1 D:HIS92 4.6 97.3 1.0 NE2 D:HIS63 4.7 0.2 1.0 CE1 D:HIS63 4.8 0.8 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