Iron in PDB 3o89: Crystal Structure of Sperm Whale Myoglobin G65T

The structure of Crystal Structure of Sperm Whale Myoglobin G65T, PDB code: 3o89 was solved by X.Huang, L.Lovelace, L.Lebioda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.99 / 1.10
Space group	P 6
Cell size a, b, c (Å), α, β, γ (°)	90.439, 90.439, 45.247, 90.00, 90.00, 120.00
R / Rfree (%)	17.2 / 18.3

The binding sites of Iron atom in the Crystal Structure of Sperm Whale Myoglobin G65T (pdb code 3o89). 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 Crystal Structure of Sperm Whale Myoglobin G65T, PDB code: 3o89:

Iron binding site 1 out of 1 in the Crystal Structure of Sperm Whale Myoglobin G65T


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 Sperm Whale Myoglobin G65T within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe2154 b:6.3 occ:1.00 FE A:HEM2154 0.0 6.3 1.0 NB A:HEM2154 2.0 6.2 1.0 ND A:HEM2154 2.0 7.0 1.0 NA A:HEM2154 2.1 6.8 1.0 NC A:HEM2154 2.1 6.8 1.0 O A:HOH4001 2.1 9.7 1.0 NE2 A:HIS2093 2.1 6.9 1.0 CE1 A:HIS2093 3.0 7.6 1.0 C1B A:HEM2154 3.0 6.5 1.0 C1D A:HEM2154 3.0 7.0 1.0 C4B A:HEM2154 3.1 6.8 1.0 C4D A:HEM2154 3.1 7.3 1.0 C4C A:HEM2154 3.1 6.9 1.0 C4A A:HEM2154 3.1 6.8 1.0 C1A A:HEM2154 3.1 7.0 1.0 C1C A:HEM2154 3.1 7.0 1.0 CD2 A:HIS2093 3.1 6.9 1.0 CHD A:HEM2154 3.4 7.4 1.0 CHB A:HEM2154 3.4 7.4 1.0 CHC A:HEM2154 3.4 7.0 1.0 CHA A:HEM2154 3.4 7.5 1.0 ND1 A:HIS2093 4.2 7.7 1.0 CG A:HIS2093 4.2 6.9 1.0 C2B A:HEM2154 4.3 6.9 1.0 C3B A:HEM2154 4.3 7.0 1.0 C3C A:HEM2154 4.3 7.2 1.0 C2D A:HEM2154 4.3 8.2 1.0 C3D A:HEM2154 4.3 8.5 1.0 C3A A:HEM2154 4.3 6.9 1.0 C2C A:HEM2154 4.3 7.3 1.0 C2A A:HEM2154 4.3 7.2 1.0 NE2 A:HIS2064 4.6 10.3 1.0 CG2 A:VAL2068 4.6 7.3 1.0 CE1 A:HIS2064 4.8 11.0 1.0 CD2 A:HIS2097 5.0 9.7 1.0

X.Huang, J.Du, J.Dawson, L.Lebioda. Investigations of Structural Factors That Influence the Mechanism of Halophenol Dehalogenation Using 'Peroxidase-Like' Myoglobin Mutants and 'Myoglobin-Like' Amphitrite Ornata Dehaloperoxidase Mutants To Be Published.