Chlorine in PDB 4kmm: M76H Variant of Human Ferrochelatase

All present enzymatic activity of M76H Variant of Human Ferrochelatase:
4.99.1.1;

The structure of M76H Variant of Human Ferrochelatase, PDB code: 4kmm was solved by W.N.Lanzilotta, A.E.Medlock, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	71.26 / 2.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	88.138, 93.418, 110.219, 90.00, 90.00, 90.00
R / Rfree (%)	20.5 / 25.9

The structure of M76H Variant of Human Ferrochelatase also contains other interesting chemical elements:

Iron

(Fe)

6 atoms

The binding sites of Chlorine atom in the M76H Variant of Human Ferrochelatase (pdb code 4kmm). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the M76H Variant of Human Ferrochelatase, PDB code: 4kmm:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the M76H Variant of Human Ferrochelatase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of M76H Variant of Human Ferrochelatase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl505 b:37.0 occ:1.00 OG A:SER130 3.1 25.6 1.0 OH A:TYR123 3.2 34.6 1.0 CB A:HIS341 3.2 26.9 1.0 CB A:SER130 3.3 25.6 1.0 CD1 A:ILE132 3.4 23.3 1.0 N A:ILE342 3.5 26.1 1.0 CE2 A:TYR123 3.9 32.4 1.0 CA A:HIS341 3.9 26.6 1.0 CG1 A:ILE132 4.0 25.8 1.0 CZ A:TYR123 4.0 34.0 1.0 CA A:GLY78 4.0 29.3 1.0 CB A:ILE342 4.1 25.9 1.0 C A:HIS341 4.2 26.3 1.0 CG A:HIS341 4.3 32.6 1.0 CG2 A:ILE342 4.3 23.8 1.0 CA A:ILE342 4.4 26.5 1.0 CA A:SER130 4.4 24.9 1.0 ND1 A:HIS341 4.5 37.1 1.0 N A:GLY78 4.6 27.7 1.0 O A:GLY77 4.9 26.7 1.0 CE1 A:HIS76 4.9 30.3 0.5 C A:GLY78 5.0 29.6 1.0 C A:GLY77 5.0 27.0 1.0 CMD A:HEM501 5.0 58.6 0.5

Chlorine binding site 2 out of 2 in the M76H Variant of Human Ferrochelatase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of M76H Variant of Human Ferrochelatase within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl505 b:49.1 occ:1.00 N B:ILE342 3.1 23.6 1.0 CB B:HIS341 3.2 24.1 1.0 OG B:SER130 3.3 28.9 1.0 OH B:TYR123 3.3 32.3 1.0 CD1 B:ILE132 3.4 25.0 1.0 CB B:SER130 3.5 28.4 1.0 CA B:HIS341 3.7 24.2 1.0 CE2 B:TYR123 3.8 30.2 1.0 CB B:ILE342 3.8 24.4 1.0 C B:HIS341 3.9 23.5 1.0 CG2 B:ILE342 4.0 22.5 1.0 CZ B:TYR123 4.0 32.1 1.0 CA B:ILE342 4.0 24.7 1.0 CG1 B:ILE132 4.1 24.7 1.0 CA B:GLY78 4.2 27.1 1.0 CG B:HIS341 4.2 29.4 1.0 CA B:SER130 4.4 28.3 1.0 ND1 B:HIS341 4.4 34.0 1.0 CMD B:HEM501 4.8 54.6 0.5 O B:GLY77 4.9 28.1 1.0

W.N.Lanzilotta, A.E.Medlock. M76H Variant of Human Ferrochelatase To Be Published.