Iron in PDB 3vre: The Crystal Structure of Hemoglobin From Woolly Mammoth in the Deoxy Form

The structure of The Crystal Structure of Hemoglobin From Woolly Mammoth in the Deoxy Form, PDB code: 3vre was solved by H.Noguchi, K.L.Campbell, C.Ho, S.-Y.Park, J.R.H.Tame, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.20
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	53.640, 59.080, 62.100, 96.72, 114.36, 113.86
R / Rfree (%)	20.3 / 26.9

The binding sites of Iron atom in the The Crystal Structure of Hemoglobin From Woolly Mammoth in the Deoxy Form (pdb code 3vre). 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 Crystal Structure of Hemoglobin From Woolly Mammoth in the Deoxy Form, PDB code: 3vre:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the The Crystal Structure of Hemoglobin From Woolly Mammoth in the Deoxy Form


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Crystal Structure of Hemoglobin From Woolly Mammoth in the Deoxy Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:33.4 occ:1.00 FE A:HEM201 0.0 33.4 1.0 NB A:HEM201 2.0 36.0 1.0 NC A:HEM201 2.1 35.4 1.0 ND A:HEM201 2.1 32.9 1.0 NA A:HEM201 2.1 35.1 1.0 NE2 A:HIS87 2.2 33.8 1.0 C1B A:HEM201 3.0 34.8 1.0 C4C A:HEM201 3.0 35.8 1.0 CE1 A:HIS87 3.0 32.6 1.0 C1D A:HEM201 3.0 33.7 1.0 C4A A:HEM201 3.1 33.2 1.0 C4B A:HEM201 3.1 35.8 1.0 C1C A:HEM201 3.1 34.7 1.0 C4D A:HEM201 3.2 34.4 1.0 C1A A:HEM201 3.2 35.5 1.0 O A:HOH326 3.2 37.5 1.0 CD2 A:HIS87 3.3 31.8 1.0 CHD A:HEM201 3.3 34.3 1.0 CHB A:HEM201 3.3 35.0 1.0 CHC A:HEM201 3.5 35.1 1.0 CHA A:HEM201 3.6 32.8 1.0 ND1 A:HIS87 4.2 30.8 1.0 C2B A:HEM201 4.2 34.8 1.0 C3C A:HEM201 4.3 35.1 1.0 C3B A:HEM201 4.3 34.9 1.0 C2C A:HEM201 4.3 34.9 1.0 C3A A:HEM201 4.3 34.5 1.0 C2D A:HEM201 4.3 33.5 1.0 C2A A:HEM201 4.4 35.6 1.0 CG A:HIS87 4.4 33.8 1.0 C3D A:HEM201 4.4 33.7 1.0 CD1 A:LEU91 4.5 30.4 1.0 CE1 A:HIS58 4.6 28.4 1.0 NE2 A:HIS58 4.7 27.9 1.0

Iron binding site 2 out of 4 in the The Crystal Structure of Hemoglobin From Woolly Mammoth in the Deoxy Form


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The Crystal Structure of Hemoglobin From Woolly Mammoth in the Deoxy Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:32.4 occ:1.00 FE B:HEM201 0.0 32.4 1.0 NA B:HEM201 2.1 32.9 1.0 NC B:HEM201 2.1 32.4 1.0 ND B:HEM201 2.1 32.6 1.0 NB B:HEM201 2.1 32.8 1.0 NE2 B:HIS92 2.2 32.8 1.0 C4B B:HEM201 3.1 33.6 1.0 C1C B:HEM201 3.1 31.2 1.0 C1A B:HEM201 3.1 32.2 1.0 C4D B:HEM201 3.1 34.1 1.0 C4A B:HEM201 3.1 33.5 1.0 C1D B:HEM201 3.1 33.5 1.0 C4C B:HEM201 3.1 32.0 1.0 C1B B:HEM201 3.1 33.8 1.0 CD2 B:HIS92 3.2 33.1 1.0 CE1 B:HIS92 3.2 32.1 1.0 CHC B:HEM201 3.4 34.0 1.0 CHA B:HEM201 3.4 30.7 1.0 CHD B:HEM201 3.5 32.6 1.0 CHB B:HEM201 3.5 32.5 1.0 NE2 B:HIS63 3.9 32.4 1.0 CG2 B:VAL67 4.1 35.3 1.0 C3B B:HEM201 4.3 34.7 1.0 C2A B:HEM201 4.3 33.6 1.0 ND1 B:HIS92 4.3 30.3 1.0 C2B B:HEM201 4.3 34.9 1.0 C2C B:HEM201 4.3 32.3 1.0 C3A B:HEM201 4.3 34.5 1.0 C3C B:HEM201 4.3 32.1 1.0 C3D B:HEM201 4.3 34.6 1.0 CG B:HIS92 4.3 33.3 1.0 C2D B:HEM201 4.4 33.6 1.0 CE1 B:HIS63 4.5 34.7 1.0 CD1 B:LEU96 5.0 33.8 1.0 CD2 B:HIS63 5.0 33.2 1.0

Iron binding site 3 out of 4 in the The Crystal Structure of Hemoglobin From Woolly Mammoth in the Deoxy Form


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of The Crystal Structure of Hemoglobin From Woolly Mammoth in the Deoxy Form within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:30.6 occ:1.00 FE C:HEM201 0.0 30.6 1.0 NA C:HEM201 2.0 31.6 1.0 NB C:HEM201 2.1 29.3 1.0 NC C:HEM201 2.1 31.5 1.0 ND C:HEM201 2.1 32.8 1.0 NE2 C:HIS87 2.2 30.1 1.0 C1D C:HEM201 3.0 32.1 1.0 C4C C:HEM201 3.0 31.9 1.0 C4A C:HEM201 3.1 31.2 1.0 C1B C:HEM201 3.1 30.4 1.0 C1A C:HEM201 3.1 33.1 1.0 C4D C:HEM201 3.1 32.4 1.0 C4B C:HEM201 3.1 32.4 1.0 C1C C:HEM201 3.1 31.5 1.0 CE1 C:HIS87 3.2 31.3 1.0 CD2 C:HIS87 3.3 31.1 1.0 O C:HOH325 3.4 35.8 1.0 CHD C:HEM201 3.4 32.6 1.0 CHB C:HEM201 3.4 29.8 1.0 CHA C:HEM201 3.5 32.2 1.0 CHC C:HEM201 3.5 30.8 1.0 CE1 C:HIS58 4.2 33.5 1.0 C3C C:HEM201 4.3 31.2 1.0 C2D C:HEM201 4.3 33.1 1.0 C3A C:HEM201 4.3 30.6 1.0 C3D C:HEM201 4.3 33.0 1.0 C2A C:HEM201 4.3 32.2 1.0 ND1 C:HIS87 4.3 28.3 1.0 C2B C:HEM201 4.3 32.5 1.0 C3B C:HEM201 4.3 32.7 1.0 C2C C:HEM201 4.3 31.3 1.0 NE2 C:HIS58 4.4 33.3 1.0 CG C:HIS87 4.4 32.0 1.0 CD1 C:LEU91 4.4 30.4 1.0 CG2 C:VAL62 4.8 30.0 1.0

Iron binding site 4 out of 4 in the The Crystal Structure of Hemoglobin From Woolly Mammoth in the Deoxy Form


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of The Crystal Structure of Hemoglobin From Woolly Mammoth in the Deoxy Form within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe201 b:33.4 occ:1.00 FE D:HEM201 0.0 33.4 1.0 NC D:HEM201 2.0 33.6 1.0 ND D:HEM201 2.1 33.6 1.0 NA D:HEM201 2.1 34.2 1.0 NB D:HEM201 2.1 33.3 1.0 NE2 D:HIS92 2.2 37.1 1.0 C4C D:HEM201 3.0 33.4 1.0 C1D D:HEM201 3.0 34.5 1.0 C4A D:HEM201 3.1 34.8 1.0 C1B D:HEM201 3.1 31.6 1.0 C4D D:HEM201 3.1 33.8 1.0 C1C D:HEM201 3.1 31.9 1.0 CE1 D:HIS92 3.1 36.0 1.0 C1A D:HEM201 3.1 35.3 1.0 C4B D:HEM201 3.1 31.3 1.0 CD2 D:HIS92 3.3 35.7 1.0 CHD D:HEM201 3.3 32.8 1.0 CHB D:HEM201 3.4 34.0 1.0 CHA D:HEM201 3.5 32.2 1.0 CHC D:HEM201 3.5 30.9 1.0 NE2 D:HIS63 4.0 33.5 1.0 CG2 D:VAL67 4.2 33.0 1.0 C3C D:HEM201 4.2 32.7 1.0 ND1 D:HIS92 4.3 35.8 1.0 C2D D:HEM201 4.3 35.8 1.0 C3A D:HEM201 4.3 35.3 1.0 C2C D:HEM201 4.3 31.7 1.0 C3D D:HEM201 4.3 36.4 1.0 C2B D:HEM201 4.3 32.0 1.0 C2A D:HEM201 4.3 35.4 1.0 C3B D:HEM201 4.3 31.0 1.0 CE1 D:HIS63 4.3 31.4 1.0 CG D:HIS92 4.4 35.3 1.0 CD1 D:LEU96 4.9 33.0 1.0

H.Noguchi, K.L.Campbell, C.Ho, S.Unzai, S.-Y.Park, J.R.H.Tame. Structures of Haemoglobin From Woolly Mammoth in Liganded and Unliganded States. Acta Crystallogr.,Sect.D V. 68 1441 2012.
ISSN: ISSN 0907-4449
PubMed: 23090393
DOI: 10.1107/S0907444912029459