Chlorine in PDB 3hcr: Human Ferrochelatase with Deuteroporphyrin and Ni Bound

All present enzymatic activity of Human Ferrochelatase with Deuteroporphyrin and Ni Bound:
4.99.1.1;

The structure of Human Ferrochelatase with Deuteroporphyrin and Ni Bound, PDB code: 3hcr was solved by A.E.Medlock, H.A.Dailey, W.N.Lanzilotta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.32 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	86.423, 92.935, 109.973, 90.00, 90.00, 90.00
R / Rfree (%)	21.5 / 25

The structure of Human Ferrochelatase with Deuteroporphyrin and Ni Bound also contains other interesting chemical elements:

Iron

(Fe)

6 atoms

The binding sites of Chlorine atom in the Human Ferrochelatase with Deuteroporphyrin and Ni Bound (pdb code 3hcr). 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 Human Ferrochelatase with Deuteroporphyrin and Ni Bound, PDB code: 3hcr:

Chlorine binding site 1 out of 1 in the Human Ferrochelatase with Deuteroporphyrin and Ni Bound


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Ferrochelatase with Deuteroporphyrin and Ni Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1 b:59.8 occ:1.00 CD A:ARG327 3.4 33.2 1.0 N B:SER902 3.6 25.9 1.0 NH1 A:ARG327 3.6 35.8 1.0 O B:HOH197 3.6 52.5 1.0 O B:THR900 3.9 20.5 1.0 NZ B:LYS915 3.9 43.8 1.0 CG A:ARG327 4.0 34.8 1.0 CA B:LEU901 4.1 24.6 1.0 CB B:SER902 4.2 30.2 1.0 CD1 B:LEU901 4.2 27.6 1.0 C B:LEU901 4.4 24.2 1.0 NE A:ARG327 4.4 33.7 1.0 O A:ARG325 4.4 33.8 1.0 OG B:SER902 4.4 34.4 1.0 CZ A:ARG327 4.4 34.4 1.0 CA B:SER902 4.5 26.1 1.0 C B:THR900 4.8 22.0 1.0 O B:SER902 4.9 25.7 1.0 N B:LEU901 4.9 21.9 1.0

A.E.Medlock, M.Carter, T.A.Dailey, H.A.Dailey, W.N.Lanzilotta. Product Release Rather Than Chelation Determines Metal Specificity For Ferrochelatase. J.Mol.Biol. V. 393 308 2009.
ISSN: ISSN 0022-2836
PubMed: 19703464
DOI: 10.1016/J.JMB.2009.08.042