Iron in PDB 1ltw: Recombinant Sperm Whale Myoglobin 29W Mutant (Oxy)

The structure of Recombinant Sperm Whale Myoglobin 29W Mutant (Oxy), PDB code: 1ltw was solved by T.Li, J.S.Olson, G.N.Phillips Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	5.00 / 1.70
Space group	P 6
Cell size a, b, c (Å), α, β, γ (°)	91.461, 91.461, 45.841, 90.00, 90.00, 120.00
R / Rfree (%)	15.8 / n/a

The binding sites of Iron atom in the Recombinant Sperm Whale Myoglobin 29W Mutant (Oxy) (pdb code 1ltw). 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 29W Mutant (Oxy), PDB code: 1ltw:

Iron binding site 1 out of 1 in the Recombinant Sperm Whale Myoglobin 29W Mutant (Oxy)


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 29W Mutant (Oxy) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe154 b:15.2 occ:1.00 FE A:HEM154 0.0 15.2 1.0 O1 A:OXY155 1.8 14.8 0.8 ND A:HEM154 1.9 14.7 1.0 NA A:HEM154 2.0 14.1 1.0 NC A:HEM154 2.0 14.8 1.0 NB A:HEM154 2.0 13.3 1.0 NE2 A:HIS93 2.3 14.9 1.0 O2 A:OXY155 2.5 15.3 0.8 C4D A:HEM154 3.0 14.3 1.0 C1D A:HEM154 3.0 15.4 1.0 C4A A:HEM154 3.0 14.1 1.0 C1C A:HEM154 3.0 14.7 1.0 C1A A:HEM154 3.0 14.6 1.0 C4C A:HEM154 3.1 14.8 1.0 C1B A:HEM154 3.1 13.9 1.0 C4B A:HEM154 3.1 13.8 1.0 CE1 A:HIS93 3.2 16.0 1.0 CD2 A:HIS93 3.3 15.9 1.0 CHD A:HEM154 3.4 14.5 1.0 CHB A:HEM154 3.4 13.8 1.0 CHC A:HEM154 3.4 14.8 1.0 CHA A:HEM154 3.4 14.9 1.0 C3D A:HEM154 4.2 15.9 1.0 C2D A:HEM154 4.3 15.9 1.0 C3A A:HEM154 4.3 14.4 1.0 C2C A:HEM154 4.3 14.7 1.0 C2A A:HEM154 4.3 14.5 1.0 C3C A:HEM154 4.3 15.7 1.0 ND1 A:HIS93 4.3 16.5 1.0 C3B A:HEM154 4.4 14.2 1.0 CG A:HIS93 4.4 15.7 1.0 C2B A:HEM154 4.4 13.5 1.0 NE2 A:HIS64 4.5 21.5 1.0 CE1 A:HIS64 4.7 20.4 1.0 CG2 A:VAL68 4.7 14.4 1.0 CH2 A:TRP29 5.0 26.7 1.0

S.Hirota, T.Li, G.N.Phillips Jr., J.S.Olson, M.Mukai, T.Kitagawa. Perturbation of the Fe-O2 Bond By Nearby Residues in Heme Pocket: Observation of Vfe-O2 Raman Bands For Oxymyoglobin Mutants J.Am.Chem.Soc. V. 118 7845 1996.
ISSN: ISSN 0002-7863