Iron in PDB 5zzf: X-Ray Structure of F43Y/H64D Sperm Whale Myoglobin

The structure of X-Ray Structure of F43Y/H64D Sperm Whale Myoglobin, PDB code: 5zzf was solved by H.Yuan, Y.W.Lin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.01 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	39.841, 49.327, 77.531, 90.00, 90.00, 90.00
R / Rfree (%)	16.6 / 21

The binding sites of Iron atom in the X-Ray Structure of F43Y/H64D Sperm Whale Myoglobin (pdb code 5zzf). 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 X-Ray Structure of F43Y/H64D Sperm Whale Myoglobin, PDB code: 5zzf:

Iron binding site 1 out of 1 in the X-Ray Structure of F43Y/H64D 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 X-Ray Structure of F43Y/H64D Sperm Whale Myoglobin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:10.0 occ:1.00 FE A:HEM201 0.0 10.0 1.0 NC A:HEM201 2.0 10.9 1.0 NA A:HEM201 2.0 11.3 1.0 NB A:HEM201 2.1 9.6 1.0 ND A:HEM201 2.1 11.5 1.0 O A:HOH309 2.1 15.5 1.0 NE2 A:HIS93 2.1 9.8 1.0 C4C A:HEM201 3.0 12.5 1.0 C1C A:HEM201 3.0 10.7 1.0 C1D A:HEM201 3.0 11.7 1.0 C1B A:HEM201 3.1 8.5 1.0 C4B A:HEM201 3.1 9.4 1.0 C4D A:HEM201 3.1 11.1 1.0 CE1 A:HIS93 3.1 9.7 1.0 C1A A:HEM201 3.1 9.8 1.0 C4A A:HEM201 3.1 8.8 1.0 CD2 A:HIS93 3.2 11.0 1.0 CHD A:HEM201 3.5 12.2 1.0 CHA A:HEM201 3.5 11.6 1.0 CHC A:HEM201 3.5 9.6 1.0 CHB A:HEM201 3.5 8.7 1.0 OH A:TYR43 3.9 6.4 0.5 O A:HOH461 4.1 28.1 1.0 ND1 A:HIS93 4.2 10.5 1.0 C2D A:HEM201 4.2 13.2 1.0 C3B A:HEM201 4.3 8.8 1.0 CG A:HIS93 4.3 9.7 1.0 C3C A:HEM201 4.3 13.3 1.0 C3D A:HEM201 4.3 14.5 1.0 C2B A:HEM201 4.3 8.8 1.0 C2A A:HEM201 4.3 10.2 1.0 C2C A:HEM201 4.4 11.8 1.0 C3A A:HEM201 4.4 9.1 1.0 CG2 A:VAL68 4.6 15.3 1.0 CZ A:TYR43 4.9 13.1 0.5

L.L.Yin, H.Yuan, C.Liu, B.He, S.Q.Gao, G.B.Wen, X.Tan, Y.W.Lin. A Rationally Designed Myoglobin Exhibits A Catalytic Dehalogenation Efficiency More Than 1000-Fold That of A Native Dehaloperoxidase Acs Catalysis V. 8 9619 2018.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.8B02979