Chlorine in PDB 7l3y: Crystal Structure of Oxy-I107E Cub Myoglobin (I107E L29H F43H Sperm Whale Myoglobin; Partial Occupancy)

The structure of Crystal Structure of Oxy-I107E Cub Myoglobin (I107E L29H F43H Sperm Whale Myoglobin; Partial Occupancy), PDB code: 7l3y was solved by I.Petrik, Y.Lu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.02 / 1.18
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	39.845, 46.982, 78.034, 90, 90, 90
R / Rfree (%)	15.7 / 19

The structure of Crystal Structure of Oxy-I107E Cub Myoglobin (I107E L29H F43H Sperm Whale Myoglobin; Partial Occupancy) also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Chlorine atom in the Crystal Structure of Oxy-I107E Cub Myoglobin (I107E L29H F43H Sperm Whale Myoglobin; Partial Occupancy) (pdb code 7l3y). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Oxy-I107E Cub Myoglobin (I107E L29H F43H Sperm Whale Myoglobin; Partial Occupancy), PDB code: 7l3y:

Chlorine binding site 1 out of 1 in the Crystal Structure of Oxy-I107E Cub Myoglobin (I107E L29H F43H Sperm Whale Myoglobin; Partial Occupancy)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Oxy-I107E Cub Myoglobin (I107E L29H F43H Sperm Whale Myoglobin; Partial Occupancy) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl203 b:20.0 occ:0.50 O A:HOH353 0.1 20.0 0.5 ND1 A:HIS82 2.7 14.3 1.0 O A:ILE75 2.8 11.8 1.0 N A:GLY80 2.8 14.7 1.0 O A:HOH466 2.9 22.8 1.0 CA A:GLY80 3.4 15.2 1.0 CE1 A:HIS82 3.5 13.9 1.0 C A:ILE75 3.6 10.6 1.0 CH2 A:TRP7 3.6 12.3 1.0 N A:LYS79 3.7 14.0 1.0 CG2 A:ILE75 3.8 11.6 1.0 CG A:HIS82 3.8 14.2 1.0 C A:LYS79 3.9 14.5 1.0 CA A:LEU76 4.0 10.2 1.0 CA A:LYS79 4.1 14.5 1.0 CB A:HIS82 4.1 14.5 1.0 CZ3 A:TRP7 4.1 12.6 1.0 N A:LEU76 4.1 10.1 1.0 O A:LEU76 4.2 11.3 1.0 C A:GLY80 4.2 15.2 1.0 C A:LYS78 4.3 14.2 1.0 C A:LEU76 4.3 10.6 1.0 CZ2 A:TRP7 4.5 12.4 1.0 CA A:ILE75 4.6 10.8 1.0 N A:HIS81 4.7 15.5 1.0 CB A:LYS78 4.7 15.3 1.0 NE2 A:HIS82 4.7 13.8 1.0 CB A:ILE75 4.8 11.1 1.0 N A:LYS78 4.8 12.7 1.0 CD2 A:HIS82 4.8 13.8 1.0 CA A:LYS78 4.9 14.0 1.0 CD2 A:LEU76 4.9 11.2 1.0 O A:GLY80 4.9 15.6 1.0 O A:LYS78 5.0 14.9 1.0 O A:LYS79 5.0 15.6 1.0

I.D.Petrik, R.Davydov, M.Kahle, B.Sandoval, S.Dwaraknath, P.Adelroth, B.Hoffman, Y.Lu. An Engineered Glutamate in Biosynthetic Models of Heme-Copper Oxidases Drives Complete Product Selectivity By Tuning the Hydrogen-Bonding Network. Biochemistry 2021.
ISSN: ISSN 0006-2960
PubMed: 33464878
DOI: 10.1021/ACS.BIOCHEM.0C00852