Iron in PDB 6z4t: Sperm Whale Myoglobin Mutant (H64V V64A) Bearing the Non-Canonical Amino Acid 2-Amino-3-(Thiazol-5-Yl)Propanoic Acid As Axial Heme Ligand

The structure of Sperm Whale Myoglobin Mutant (H64V V64A) Bearing the Non-Canonical Amino Acid 2-Amino-3-(Thiazol-5-Yl)Propanoic Acid As Axial Heme Ligand, PDB code: 6z4t was solved by M.Tinzl, D.Hilvert, P.R.E.Mittl, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.31 / 1.23
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	40.009, 47.327, 76.897, 90, 90, 90
R / Rfree (%)	15 / 18.8

The binding sites of Iron atom in the Sperm Whale Myoglobin Mutant (H64V V64A) Bearing the Non-Canonical Amino Acid 2-Amino-3-(Thiazol-5-Yl)Propanoic Acid As Axial Heme Ligand (pdb code 6z4t). 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 Sperm Whale Myoglobin Mutant (H64V V64A) Bearing the Non-Canonical Amino Acid 2-Amino-3-(Thiazol-5-Yl)Propanoic Acid As Axial Heme Ligand, PDB code: 6z4t:

Iron binding site 1 out of 1 in the Sperm Whale Myoglobin Mutant (H64V V64A) Bearing the Non-Canonical Amino Acid 2-Amino-3-(Thiazol-5-Yl)Propanoic Acid As Axial Heme Ligand


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Sperm Whale Myoglobin Mutant (H64V V64A) Bearing the Non-Canonical Amino Acid 2-Amino-3-(Thiazol-5-Yl)Propanoic Acid As Axial Heme Ligand within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1201 b:14.1 occ:1.00 FE A:HEM1201 0.0 14.1 1.0 O1 A:OXY1202 1.9 19.0 1.0 NB A:HEM1201 2.0 13.2 1.0 ND A:HEM1201 2.0 15.7 1.0 NA A:HEM1201 2.0 15.8 1.0 NC A:HEM1201 2.0 13.6 1.0 NZ A:Q7593 2.3 15.0 1.0 C1D A:HEM1201 3.0 16.0 1.0 C4A A:HEM1201 3.0 14.0 1.0 C1B A:HEM1201 3.1 12.0 1.0 C4B A:HEM1201 3.1 12.6 1.0 C1A A:HEM1201 3.1 15.9 1.0 C4C A:HEM1201 3.1 13.4 1.0 C4D A:HEM1201 3.1 16.1 1.0 C1C A:HEM1201 3.1 13.5 1.0 CE A:Q7593 3.1 15.4 1.0 O2 A:OXY1202 3.1 22.1 1.0 CD A:Q7593 3.3 14.6 1.0 CHD A:HEM1201 3.4 15.3 1.0 CHB A:HEM1201 3.4 12.8 1.0 CHC A:HEM1201 3.4 13.2 1.0 CHA A:HEM1201 3.4 17.0 1.0 C3A A:HEM1201 4.3 15.4 1.0 C2A A:HEM1201 4.3 16.1 1.0 C2D A:HEM1201 4.3 17.1 1.0 C3B A:HEM1201 4.3 13.0 1.0 C3C A:HEM1201 4.3 13.5 1.0 C2B A:HEM1201 4.3 12.0 1.0 C3D A:HEM1201 4.3 17.4 1.0 C2C A:HEM1201 4.3 13.6 1.0 O A:HOH1380 4.4 33.0 1.0 CG A:Q7593 4.4 13.7 1.0 SD A:Q7593 4.5 13.6 1.0 CB A:ALA68 4.9 12.6 1.0

M.Pott, M.Tinzl, T.Hayashi, Y.Ota, D.Dunkelmann, P.R.E.Mittl, D.Hilvert. Noncanonical Heme Ligands Steer Carbene Transfer Reactivity in An Artificial Metalloenzyme. Angew.Chem.Int.Ed.Engl. 2021.
ISSN: ESSN 1521-3773
PubMed: 33880851
DOI: 10.1002/ANIE.202103437