Iron in PDB 1cp0: Recombinant Sperm Whale Myoglobin L104N Mutant (Met)

The structure of Recombinant Sperm Whale Myoglobin L104N Mutant (Met), PDB code: 1cp0 was solved by E.C.Liong, 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 / 2.00
Space group	P 6
Cell size a, b, c (Å), α, β, γ (°)	91.468, 91.468, 45.903, 90.00, 90.00, 120.00
R / Rfree (%)	14.1 / 20.2

The binding sites of Iron atom in the Recombinant Sperm Whale Myoglobin L104N Mutant (Met) (pdb code 1cp0). 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 L104N Mutant (Met), PDB code: 1cp0:

Iron binding site 1 out of 1 in the Recombinant Sperm Whale Myoglobin L104N 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 L104N Mutant (Met) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe154 b:16.5 occ:1.00 FE A:HEM154 0.0 16.5 1.0 ND A:HEM154 2.0 15.1 1.0 NA A:HEM154 2.0 11.2 1.0 NC A:HEM154 2.0 13.0 1.0 NB A:HEM154 2.0 15.9 1.0 NE2 A:HIS93 2.2 17.4 1.0 O A:HOH155 2.2 15.3 1.0 C4D A:HEM154 3.0 12.0 1.0 C4A A:HEM154 3.0 12.4 1.0 C1D A:HEM154 3.0 12.0 1.0 C4C A:HEM154 3.0 14.1 1.0 C1C A:HEM154 3.0 12.1 1.0 C1A A:HEM154 3.0 12.9 1.0 C1B A:HEM154 3.0 12.0 1.0 C4B A:HEM154 3.0 12.8 1.0 CE1 A:HIS93 3.1 14.3 1.0 CD2 A:HIS93 3.1 21.5 1.0 CHB A:HEM154 3.4 12.0 1.0 CHA A:HEM154 3.4 13.4 1.0 CHD A:HEM154 3.4 15.4 1.0 CHC A:HEM154 3.4 16.1 1.0 C3D A:HEM154 4.2 9.6 1.0 C2A A:HEM154 4.2 14.0 1.0 C3A A:HEM154 4.2 15.8 1.0 C2D A:HEM154 4.2 12.5 1.0 C3C A:HEM154 4.2 18.2 1.0 C2C A:HEM154 4.2 14.5 1.0 C2B A:HEM154 4.2 16.6 1.0 ND1 A:HIS93 4.2 15.2 1.0 C3B A:HEM154 4.3 14.2 1.0 CG A:HIS93 4.3 16.1 1.0 NE2 A:HIS64 4.4 17.3 1.0 CE1 A:HIS64 4.8 15.1 1.0 CG2 A:VAL68 4.8 20.9 1.0

E.C.Liong, Y.Dou, E.E.Scott, J.S.Olson, G.N.Phillips Jr.. Waterproofing the Heme Pocket. Role of Proximal Amino Acid Side Chains in Preventing Hemin Loss From Myoglobin. J.Biol.Chem. V. 276 9093 2001.
ISSN: ISSN 0021-9258
PubMed: 11084036
DOI: 10.1074/JBC.M008593200