Iron in PDB 2hrc: 1.7 Angstrom Structure of Human Ferrochelatase Variant R115L

All present enzymatic activity of 1.7 Angstrom Structure of Human Ferrochelatase Variant R115L:
4.99.1.1;

The structure of 1.7 Angstrom Structure of Human Ferrochelatase Variant R115L, PDB code: 2hrc was solved by A.Medlock, L.Swartz, T.A.Dailey, 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)	41.84 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	88.526, 92.983, 110.454, 90.00, 90.00, 90.00
R / Rfree (%)	22.1 / 24.2

The structure of 1.7 Angstrom Structure of Human Ferrochelatase Variant R115L also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Iron atom in the 1.7 Angstrom Structure of Human Ferrochelatase Variant R115L (pdb code 2hrc). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the 1.7 Angstrom Structure of Human Ferrochelatase Variant R115L, PDB code: 2hrc:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the 1.7 Angstrom Structure of Human Ferrochelatase Variant R115L


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of 1.7 Angstrom Structure of Human Ferrochelatase Variant R115L within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1501 b:16.0 occ:1.00 FE1 A:FES1501 0.0 16.0 1.0 S1 A:FES1501 2.2 16.2 1.0 S2 A:FES1501 2.2 17.0 1.0 SG A:CYS196 2.3 16.9 1.0 SG A:CYS403 2.4 16.6 1.0 FE2 A:FES1501 2.7 16.2 1.0 CB A:CYS403 3.4 17.1 1.0 CB A:CYS196 3.4 15.3 1.0 O A:HOH1798 3.5 31.2 1.0 N A:CYS403 3.9 17.6 1.0 O A:HOH1795 3.9 31.8 1.0 CA A:CYS403 4.2 17.4 1.0 O A:HOH1640 4.3 24.1 1.0 CB A:CYS406 4.4 19.4 1.0 SG A:CYS406 4.6 18.3 1.0 SG A:CYS411 4.6 19.8 1.0 CA A:CYS196 4.7 15.1 1.0 NE A:ARG272 4.9 16.6 0.5 NH2 B:ARG798 4.9 17.1 1.0

Iron binding site 2 out of 4 in the 1.7 Angstrom Structure of Human Ferrochelatase Variant R115L


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of 1.7 Angstrom Structure of Human Ferrochelatase Variant R115L within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1501 b:16.2 occ:1.00 FE2 A:FES1501 0.0 16.2 1.0 S2 A:FES1501 2.2 17.0 1.0 S1 A:FES1501 2.2 16.2 1.0 SG A:CYS406 2.4 18.3 1.0 SG A:CYS411 2.4 19.8 1.0 FE1 A:FES1501 2.7 16.0 1.0 CB A:CYS411 3.2 20.5 1.0 CB A:CYS406 3.2 19.4 1.0 O A:HOH1678 4.2 24.4 1.0 CA A:CYS406 4.2 19.8 1.0 O A:HOH1795 4.3 31.8 1.0 O A:HOH1775 4.3 25.9 1.0 O A:HOH1797 4.4 39.4 1.0 SG A:CYS196 4.6 16.9 1.0 CB A:ASN408 4.6 22.8 1.0 O A:ASN408 4.6 22.2 1.0 CA A:CYS411 4.7 20.8 1.0 SG A:CYS403 4.7 16.6 1.0 N A:CYS403 4.8 17.6 1.0 CB A:CYS403 4.8 17.1 1.0 CB A:CYS196 4.9 15.3 1.0 CB A:SER402 4.9 18.3 1.0 N A:ASN408 5.0 22.4 1.0

Iron binding site 3 out of 4 in the 1.7 Angstrom Structure of Human Ferrochelatase Variant R115L


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of 1.7 Angstrom Structure of Human Ferrochelatase Variant R115L within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1502 b:16.6 occ:1.00 FE1 B:FES1502 0.0 16.6 1.0 S1 B:FES1502 2.2 16.4 1.0 S2 B:FES1502 2.2 17.5 1.0 SG B:CYS696 2.3 17.9 1.0 SG B:CYS903 2.4 18.3 1.0 FE2 B:FES1502 2.7 16.7 1.0 CB B:CYS903 3.3 18.4 1.0 CB B:CYS696 3.4 16.6 1.0 O B:HOH1832 3.7 29.2 1.0 N B:CYS903 3.9 18.4 1.0 O B:HOH1813 3.9 35.2 1.0 CA B:CYS903 4.2 18.5 1.0 O B:HOH1646 4.4 24.2 1.0 CB B:CYS906 4.5 20.4 1.0 SG B:CYS906 4.6 19.0 1.0 SG B:CYS911 4.6 20.2 1.0 CA B:CYS696 4.7 16.5 1.0 NE B:ARG772 4.9 18.3 0.5 NH2 A:ARG298 4.9 17.8 1.0

Iron binding site 4 out of 4 in the 1.7 Angstrom Structure of Human Ferrochelatase Variant R115L


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of 1.7 Angstrom Structure of Human Ferrochelatase Variant R115L within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1502 b:16.7 occ:1.00 FE2 B:FES1502 0.0 16.7 1.0 S2 B:FES1502 2.2 17.5 1.0 S1 B:FES1502 2.2 16.4 1.0 SG B:CYS906 2.4 19.0 1.0 SG B:CYS911 2.4 20.2 1.0 FE1 B:FES1502 2.7 16.6 1.0 CB B:CYS911 3.2 20.6 1.0 CB B:CYS906 3.2 20.4 1.0 O B:HOH1695 4.2 25.8 1.0 O B:HOH1813 4.2 35.2 1.0 O B:HOH1781 4.2 31.6 1.0 CA B:CYS906 4.2 20.8 1.0 SG B:CYS696 4.5 17.9 1.0 CB B:ASN908 4.6 23.6 1.0 O B:ASN908 4.6 23.2 1.0 CA B:CYS911 4.7 20.8 1.0 SG B:CYS903 4.7 18.3 1.0 CB B:CYS903 4.8 18.4 1.0 N B:CYS903 4.8 18.4 1.0 CB B:CYS696 4.9 16.6 1.0 CB B:SER902 4.9 18.7 1.0 N B:ASN908 5.0 23.2 1.0

A.Medlock, L.Swartz, T.A.Dailey, H.A.Dailey, W.N.Lanzilotta. Substrate Interactions with Human Ferrochelatase Proc.Natl.Acad.Sci.Usa V. 104 1789 2007.
ISSN: ISSN 0027-8424
PubMed: 17261801
DOI: 10.1073/PNAS.0606144104