Iron in PDB 2spn: A Novel Site-Directed Mutant of Myoglobin with An Unusually High O2 Affinity and Low Autooxidation Rate

The structure of A Novel Site-Directed Mutant of Myoglobin with An Unusually High O2 Affinity and Low Autooxidation Rate, PDB code: 2spn was solved by M.L.Quillin, R.M.Arduini, 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 (°)	91.200, 91.200, 45.870, 90.00, 90.00, 120.00
R / Rfree (%)	n/a / n/a

The binding sites of Iron atom in the A Novel Site-Directed Mutant of Myoglobin with An Unusually High O2 Affinity and Low Autooxidation Rate (pdb code 2spn). 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 A Novel Site-Directed Mutant of Myoglobin with An Unusually High O2 Affinity and Low Autooxidation Rate, PDB code: 2spn:

Iron binding site 1 out of 1 in the A Novel Site-Directed Mutant of Myoglobin with An Unusually High O2 Affinity and Low Autooxidation Rate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of A Novel Site-Directed Mutant of Myoglobin with An Unusually High O2 Affinity and Low Autooxidation Rate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe154 b:11.3 occ:1.00 FE A:HEM154 0.0 11.3 1.0 O1 A:OXY155 1.9 13.2 1.0 ND A:HEM154 2.0 12.6 1.0 NB A:HEM154 2.0 11.2 1.0 NC A:HEM154 2.1 9.9 1.0 NA A:HEM154 2.1 10.8 1.0 NE2 A:HIS93 2.3 8.5 1.0 O2 A:OXY155 2.8 19.6 1.0 C4B A:HEM154 3.0 11.0 1.0 C4D A:HEM154 3.0 12.5 1.0 C1D A:HEM154 3.0 13.5 1.0 C1C A:HEM154 3.0 9.7 1.0 C1A A:HEM154 3.0 11.6 1.0 C1B A:HEM154 3.0 12.8 1.0 C4A A:HEM154 3.1 11.1 1.0 C4C A:HEM154 3.1 10.8 1.0 CE1 A:HIS93 3.1 12.1 1.0 CD2 A:HIS93 3.1 11.4 1.0 CHC A:HEM154 3.4 12.5 1.0 CHA A:HEM154 3.4 13.6 1.0 CHB A:HEM154 3.4 12.3 1.0 CHD A:HEM154 3.5 11.8 1.0 C3D A:HEM154 4.3 12.0 1.0 C2D A:HEM154 4.3 11.6 1.0 C3B A:HEM154 4.3 11.1 1.0 ND1 A:HIS93 4.3 8.9 1.0 C2B A:HEM154 4.3 12.1 1.0 C2C A:HEM154 4.3 10.6 1.0 C2A A:HEM154 4.3 11.6 1.0 C3A A:HEM154 4.3 10.2 1.0 C3C A:HEM154 4.3 11.4 1.0 CG A:HIS93 4.3 8.6 1.0 NE2 A:HIS64 4.5 17.1 1.0 CG2 A:VAL68 4.5 6.4 1.0 CE1 A:HIS64 4.6 15.3 1.0

T.E.Carver, R.E.Brantley Jr., E.W.Singleton, R.M.Arduini, M.L.Quillin, G.N.Phillips Jr., J.S.Olson. A Novel Site-Directed Mutant of Myoglobin with An Unusually High O2 Affinity and Low Autooxidation Rate. J.Biol.Chem. V. 267 14443 1992.
ISSN: ISSN 0021-9258
PubMed: 1629229