Iron in PDB 1wla: Myoglobin (Horse Heart) Recombinant Wild-Type

The structure of Myoglobin (Horse Heart) Recombinant Wild-Type, PDB code: 1wla was solved by R.Maurus, G.D.Brayer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 1.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	64.296, 28.966, 35.933, 90.00, 107.19, 90.00
R / Rfree (%)	16 / n/a

The binding sites of Iron atom in the Myoglobin (Horse Heart) Recombinant Wild-Type (pdb code 1wla). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Myoglobin (Horse Heart) Recombinant Wild-Type, PDB code: 1wla:

Iron binding site 1 out of 1 in the Myoglobin (Horse Heart) Recombinant Wild-Type


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Myoglobin (Horse Heart) Recombinant Wild-Type within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe154 b:8.0 occ:1.00 FE A:HEM154 0.0 8.0 1.0 NB A:HEM154 2.0 4.2 1.0 NA A:HEM154 2.0 5.0 1.0 ND A:HEM154 2.0 6.2 1.0 NC A:HEM154 2.0 5.3 1.0 NE2 A:HIS93 2.1 4.9 1.0 O A:HOH156 2.2 8.3 1.0 C4A A:HEM154 3.0 6.7 1.0 C4B A:HEM154 3.0 7.3 1.0 C1A A:HEM154 3.0 5.3 1.0 C4C A:HEM154 3.0 5.8 1.0 C1C A:HEM154 3.0 5.8 1.0 CE1 A:HIS93 3.1 5.6 1.0 C4D A:HEM154 3.1 6.9 1.0 C1B A:HEM154 3.1 4.2 1.0 C1D A:HEM154 3.1 5.9 1.0 CD2 A:HIS93 3.2 5.9 1.0 CHC A:HEM154 3.3 5.8 1.0 CHB A:HEM154 3.4 4.0 1.0 CHA A:HEM154 3.4 6.2 1.0 CHD A:HEM154 3.4 5.2 1.0 ND1 A:HIS93 4.2 7.4 1.0 C3A A:HEM154 4.2 6.1 1.0 C2A A:HEM154 4.2 6.1 1.0 C3B A:HEM154 4.3 6.7 1.0 C2B A:HEM154 4.3 5.7 1.0 C3D A:HEM154 4.3 8.1 1.0 CG A:HIS93 4.3 7.1 1.0 C2D A:HEM154 4.3 6.6 1.0 C2C A:HEM154 4.3 7.5 1.0 C3C A:HEM154 4.3 6.7 1.0 NE2 A:HIS64 4.4 6.6 1.0 CG2 A:VAL68 4.7 4.6 1.0 CE1 A:HIS64 4.8 8.4 1.0

R.Maurus, C.M.Overall, R.Bogumil, Y.Luo, A.G.Mauk, M.Smith, G.D.Brayer. A Myoglobin Variant with A Polar Substitution in A Conserved Hydrophobic Cluster in the Heme Binding Pocket. Biochim.Biophys.Acta V.1341 1 1997.
ISSN: ISSN 0006-3002
PubMed: 9300804
DOI: 10.1016/S0167-4838(97)00064-2