Iron in PDB 1lue: Recombinant Sperm Whale Myoglobin H64D/V68A/D122N Mutant (Met)

The structure of Recombinant Sperm Whale Myoglobin H64D/V68A/D122N Mutant (Met), PDB code: 1lue was solved by G.N.Phillips Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	18.12 / 1.70
Space group	P 6
Cell size a, b, c (Å), α, β, γ (°)	91.200, 91.200, 45.850, 90.00, 90.00, 120.00
R / Rfree (%)	16.8 / 20.2

The binding sites of Iron atom in the Recombinant Sperm Whale Myoglobin H64D/V68A/D122N Mutant (Met) (pdb code 1lue). 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 Recombinant Sperm Whale Myoglobin H64D/V68A/D122N Mutant (Met), PDB code: 1lue:

Iron binding site 1 out of 1 in the Recombinant Sperm Whale Myoglobin H64D/V68A/D122N Mutant (Met)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Recombinant Sperm Whale Myoglobin H64D/V68A/D122N Mutant (Met) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe154 b:4.9 occ:1.00 FE A:HEM154 0.0 4.9 1.0 NB A:HEM154 2.0 3.6 1.0 NA A:HEM154 2.0 3.5 1.0 ND A:HEM154 2.0 4.7 1.0 NC A:HEM154 2.0 3.6 1.0 NE2 A:HIS93 2.1 3.1 1.0 O A:HOH155 2.2 6.4 1.0 C1B A:HEM154 3.0 2.8 1.0 C4A A:HEM154 3.0 3.4 1.0 C4B A:HEM154 3.0 4.0 1.0 C1A A:HEM154 3.0 3.8 1.0 C1C A:HEM154 3.0 3.4 1.0 C1D A:HEM154 3.0 5.8 1.0 C4D A:HEM154 3.0 6.7 1.0 C4C A:HEM154 3.0 3.2 1.0 CE1 A:HIS93 3.1 3.1 1.0 CD2 A:HIS93 3.1 4.1 1.0 CHB A:HEM154 3.4 2.3 1.0 CHC A:HEM154 3.4 4.7 1.0 CHD A:HEM154 3.4 3.9 1.0 CHA A:HEM154 3.4 5.2 1.0 ND1 A:HIS93 4.2 3.1 1.0 CG A:HIS93 4.2 2.2 1.0 C2B A:HEM154 4.2 2.1 1.0 C3B A:HEM154 4.2 3.8 1.0 C3A A:HEM154 4.2 2.3 1.0 C2A A:HEM154 4.3 3.6 1.0 C2D A:HEM154 4.3 5.9 1.0 C3D A:HEM154 4.3 4.9 1.0 C2C A:HEM154 4.3 6.4 1.0 C3C A:HEM154 4.3 5.3 1.0 O A:HOH199 4.3 7.2 1.0

H.J.Yang, T.Matsui, S.Ozaki, S.Kato, T.Ueno, G.N.Phillips Jr., S.Fukuzumi, Y.Watanabe. Molecular Engineering of Myoglobin: Influence of Residue 68 on the Rate and the Enantioselectivity of Oxidation Reactions Catalyzed By H64D/V68X Myoglobin Biochemistry V. 42 10174 2003.
ISSN: ISSN 0006-2960
PubMed: 12939145
DOI: 10.1021/BI034605U