Iron in PDB 1cmy: The Mutation BETA99 Asp-Tyr Stabilizes Y-A New, Composite Quaternary State of Human Hemoglobin

The structure of The Mutation BETA99 Asp-Tyr Stabilizes Y-A New, Composite Quaternary State of Human Hemoglobin, PDB code: 1cmy was solved by F.R.Smith, E.E.Lattman, C.W.Carter Junior, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	N/A / 3.00
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	93.100, 93.100, 144.600, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Iron atom in the The Mutation BETA99 Asp-Tyr Stabilizes Y-A New, Composite Quaternary State of Human Hemoglobin (pdb code 1cmy). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the The Mutation BETA99 Asp-Tyr Stabilizes Y-A New, Composite Quaternary State of Human Hemoglobin, PDB code: 1cmy:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the The Mutation BETA99 Asp-Tyr Stabilizes Y-A New, Composite Quaternary State of Human Hemoglobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Mutation BETA99 Asp-Tyr Stabilizes Y-A New, Composite Quaternary State of Human Hemoglobin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe142 b:15.0 occ:1.00 FE A:HEM142 0.0 15.0 1.0 NC A:HEM142 2.0 15.0 1.0 NB A:HEM142 2.0 15.0 1.0 ND A:HEM142 2.0 15.0 1.0 NA A:HEM142 2.0 15.0 1.0 NE2 A:HIS87 2.0 15.0 1.0 CE1 A:HIS87 2.8 15.0 1.0 C1D A:HEM142 3.0 15.0 1.0 C4C A:HEM142 3.0 15.0 1.0 C1C A:HEM142 3.0 15.0 1.0 C1B A:HEM142 3.0 15.0 1.0 C4D A:HEM142 3.0 15.0 1.0 C4A A:HEM142 3.0 15.0 1.0 C4B A:HEM142 3.0 15.0 1.0 C1A A:HEM142 3.1 15.0 1.0 CD2 A:HIS87 3.2 15.0 1.0 CHB A:HEM142 3.4 15.0 1.0 CHD A:HEM142 3.4 15.0 1.0 CHA A:HEM142 3.4 15.0 1.0 CHC A:HEM142 3.4 15.0 1.0 ND1 A:HIS87 4.0 15.0 1.0 CG A:HIS87 4.2 15.0 1.0 NE2 A:HIS58 4.2 15.0 1.0 C3C A:HEM142 4.3 15.0 1.0 C2C A:HEM142 4.3 15.0 1.0 C3D A:HEM142 4.3 15.0 1.0 C2D A:HEM142 4.3 15.0 1.0 C2B A:HEM142 4.3 15.0 1.0 C3B A:HEM142 4.3 15.0 1.0 C3A A:HEM142 4.3 15.0 1.0 C2A A:HEM142 4.3 15.0 1.0 CG2 A:VAL62 4.4 15.0 1.0 CE1 A:HIS58 4.8 15.0 1.0

Iron binding site 2 out of 4 in the The Mutation BETA99 Asp-Tyr Stabilizes Y-A New, Composite Quaternary State of Human Hemoglobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The Mutation BETA99 Asp-Tyr Stabilizes Y-A New, Composite Quaternary State of Human Hemoglobin within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe147 b:15.0 occ:1.00 FE B:HEM147 0.0 15.0 1.0 NB B:HEM147 2.0 15.0 1.0 NA B:HEM147 2.0 15.0 1.0 NC B:HEM147 2.0 15.0 1.0 ND B:HEM147 2.0 15.0 1.0 NE2 B:HIS92 2.0 15.0 1.0 CE1 B:HIS92 3.0 15.0 1.0 C1B B:HEM147 3.0 15.0 1.0 C4B B:HEM147 3.0 15.0 1.0 C1A B:HEM147 3.0 15.0 1.0 C4A B:HEM147 3.0 15.0 1.0 C4D B:HEM147 3.0 15.0 1.0 C1D B:HEM147 3.0 15.0 1.0 CD2 B:HIS92 3.0 15.0 1.0 C1C B:HEM147 3.0 15.0 1.0 C4C B:HEM147 3.1 15.0 1.0 CHB B:HEM147 3.4 15.0 1.0 CHC B:HEM147 3.4 15.0 1.0 CHA B:HEM147 3.4 15.0 1.0 CHD B:HEM147 3.4 15.0 1.0 ND1 B:HIS92 4.1 15.0 1.0 CG B:HIS92 4.2 15.0 1.0 C3A B:HEM147 4.2 15.0 1.0 C2B B:HEM147 4.2 15.0 1.0 C3B B:HEM147 4.2 15.0 1.0 C2D B:HEM147 4.2 15.0 1.0 C3D B:HEM147 4.2 15.0 1.0 C2A B:HEM147 4.2 15.0 1.0 C2C B:HEM147 4.3 15.0 1.0 C3C B:HEM147 4.3 15.0 1.0 NE2 B:HIS63 4.3 15.0 1.0 CG2 B:VAL67 4.7 15.0 1.0

Iron binding site 3 out of 4 in the The Mutation BETA99 Asp-Tyr Stabilizes Y-A New, Composite Quaternary State of Human Hemoglobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of The Mutation BETA99 Asp-Tyr Stabilizes Y-A New, Composite Quaternary State of Human Hemoglobin within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe142 b:15.0 occ:1.00 FE C:HEM142 0.0 15.0 1.0 ND C:HEM142 2.0 15.0 1.0 NC C:HEM142 2.0 15.0 1.0 NB C:HEM142 2.0 15.0 1.0 NA C:HEM142 2.0 15.0 1.0 NE2 C:HIS87 2.1 15.0 1.0 CE1 C:HIS87 2.9 15.0 1.0 C1D C:HEM142 3.0 15.0 1.0 C4D C:HEM142 3.0 15.0 1.0 C4C C:HEM142 3.0 15.0 1.0 C4A C:HEM142 3.0 15.0 1.0 C1C C:HEM142 3.1 15.0 1.0 C1B C:HEM142 3.1 15.0 1.0 C4B C:HEM142 3.1 15.0 1.0 C1A C:HEM142 3.1 15.0 1.0 CD2 C:HIS87 3.2 15.0 1.0 CHD C:HEM142 3.4 15.0 1.0 CHB C:HEM142 3.4 15.0 1.0 CHC C:HEM142 3.4 15.0 1.0 CHA C:HEM142 3.4 15.0 1.0 NE2 C:HIS58 4.1 15.0 1.0 ND1 C:HIS87 4.1 15.0 1.0 C2D C:HEM142 4.3 15.0 1.0 C3D C:HEM142 4.3 15.0 1.0 C3C C:HEM142 4.3 15.0 1.0 CG C:HIS87 4.3 15.0 1.0 C2C C:HEM142 4.3 15.0 1.0 C2A C:HEM142 4.3 15.0 1.0 C3B C:HEM142 4.3 15.0 1.0 C3A C:HEM142 4.3 15.0 1.0 C2B C:HEM142 4.3 15.0 1.0 CG2 C:VAL62 4.5 15.0 1.0 CE1 C:HIS58 4.9 15.0 1.0

Iron binding site 4 out of 4 in the The Mutation BETA99 Asp-Tyr Stabilizes Y-A New, Composite Quaternary State of Human Hemoglobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of The Mutation BETA99 Asp-Tyr Stabilizes Y-A New, Composite Quaternary State of Human Hemoglobin within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe147 b:15.0 occ:1.00 FE D:HEM147 0.0 15.0 1.0 NE2 D:HIS92 2.0 15.0 1.0 ND D:HEM147 2.0 15.0 1.0 NA D:HEM147 2.0 15.0 1.0 NB D:HEM147 2.0 15.0 1.0 NC D:HEM147 2.0 15.0 1.0 CE1 D:HIS92 2.6 15.0 1.0 C4A D:HEM147 3.0 15.0 1.0 C4D D:HEM147 3.0 15.0 1.0 C1A D:HEM147 3.0 15.0 1.0 C1D D:HEM147 3.0 15.0 1.0 C4B D:HEM147 3.0 15.0 1.0 C1B D:HEM147 3.0 15.0 1.0 C1C D:HEM147 3.0 15.0 1.0 C4C D:HEM147 3.1 15.0 1.0 CD2 D:HIS92 3.2 15.0 1.0 CHA D:HEM147 3.4 15.0 1.0 CHB D:HEM147 3.4 15.0 1.0 CHC D:HEM147 3.4 15.0 1.0 CHD D:HEM147 3.4 15.0 1.0 ND1 D:HIS92 3.9 15.0 1.0 CG D:HIS92 4.2 15.0 1.0 C3D D:HEM147 4.2 15.0 1.0 C3A D:HEM147 4.2 15.0 1.0 C2A D:HEM147 4.2 15.0 1.0 C2D D:HEM147 4.2 15.0 1.0 C3B D:HEM147 4.3 15.0 1.0 C2B D:HEM147 4.3 15.0 1.0 C2C D:HEM147 4.3 15.0 1.0 C3C D:HEM147 4.3 15.0 1.0 NE2 D:HIS63 4.3 15.0 1.0 CG2 D:VAL67 4.4 15.0 1.0 CE1 D:HIS63 4.9 15.0 1.0

F.R.Smith, E.E.Lattman, C.W.Carter Jr.. The Mutation Beta 99 Asp-Tyr Stabilizes Y--A New, Composite Quaternary State of Human Hemoglobin. Proteins V. 10 81 1991.
ISSN: ISSN 0887-3585
PubMed: 1896430
DOI: 10.1002/PROT.340100202