Iron in PDB 6d45: L89S Mutant of Febmb Sperm Whale Myoglobin

The structure of L89S Mutant of Febmb Sperm Whale Myoglobin, PDB code: 6d45 was solved by A.Bhagi-Damodaran, E.N.Mirts, B.Sandoval, Y.Lu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.16 / 1.78
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	39.359, 48.075, 78.237, 90.00, 90.00, 90.00
R / Rfree (%)	16.4 / 20.5

The binding sites of Iron atom in the L89S Mutant of Febmb Sperm Whale Myoglobin (pdb code 6d45). 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 L89S Mutant of Febmb Sperm Whale Myoglobin, PDB code: 6d45:

Iron binding site 1 out of 1 in the L89S Mutant of Febmb Sperm Whale Myoglobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of L89S Mutant of Febmb Sperm Whale Myoglobin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:17.7 occ:1.00 FE A:HEM201 0.0 17.7 1.0 ND A:HEM201 1.9 19.5 1.0 NA A:HEM201 2.0 14.7 1.0 NB A:HEM201 2.1 15.2 1.0 NC A:HEM201 2.1 16.1 1.0 NE2 A:HIS93 2.3 19.4 1.0 C4D A:HEM201 2.9 19.3 1.0 OE1 A:GLU68 2.9 27.2 1.0 C1D A:HEM201 2.9 18.8 1.0 C1A A:HEM201 3.0 17.1 1.0 C4A A:HEM201 3.0 17.6 1.0 C4B A:HEM201 3.0 15.6 1.0 C1B A:HEM201 3.0 16.2 1.0 C4C A:HEM201 3.1 17.2 1.0 C1C A:HEM201 3.1 16.3 1.0 CE1 A:HIS93 3.1 21.7 1.0 CHA A:HEM201 3.3 19.6 1.0 CD2 A:HIS93 3.4 19.9 1.0 CHB A:HEM201 3.4 15.9 1.0 CHC A:HEM201 3.4 18.1 1.0 CHD A:HEM201 3.4 17.0 1.0 CD A:GLU68 3.7 23.9 1.0 CG A:GLU68 4.0 18.2 1.0 C2A A:HEM201 4.2 17.9 1.0 C3A A:HEM201 4.2 17.2 1.0 C2D A:HEM201 4.2 20.1 1.0 C3D A:HEM201 4.2 22.9 1.0 C2B A:HEM201 4.2 18.6 1.0 C3B A:HEM201 4.3 17.4 1.0 ND1 A:HIS93 4.3 20.2 1.0 C3C A:HEM201 4.3 17.0 1.0 C2C A:HEM201 4.3 16.4 1.0 CE1 A:HIS64 4.4 22.5 1.0 CG A:HIS93 4.4 17.4 1.0 NE2 A:HIS64 4.5 26.7 1.0 OE2 A:GLU68 4.8 26.9 1.0 O A:HOH376 4.9 23.9 1.0

A.Bhagi-Damodaran, J.H.Reed, Q.Zhu, Y.Shi, P.Hosseinzadeh, B.A.Sandoval, K.A.Harnden, S.Wang, M.R.Sponholtz, E.N.Mirts, S.Dwaraknath, Y.Zhang, P.Moenne-Loccoz, Y.Lu. Heme Redox Potentials Hold the Key to Reactivity Differences Between Nitric Oxide Reductase and Heme-Copper Oxidase. Proc. Natl. Acad. Sci. V. 115 6195 2018U.S.A..
ISSN: ESSN 1091-6490
PubMed: 29802230
DOI: 10.1073/PNAS.1720298115