Iron in PDB 1hrk: Crystal Structure of Human Ferrochelatase

All present enzymatic activity of Crystal Structure of Human Ferrochelatase:
4.99.1.1;

The structure of Crystal Structure of Human Ferrochelatase, PDB code: 1hrk was solved by C.K.Wu, H.A.Dailey, J.P.Rose, A.Burden, V.M.Sellers, B.-C.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.87 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	93.433, 87.569, 109.699, 90.00, 90.00, 90.00
R / Rfree (%)	20.2 / 22.6

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

Iron binding site 1 out of 4 in the Crystal Structure of Human Ferrochelatase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Human Ferrochelatase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1499 b:13.9 occ:1.00 FE1 A:FES1499 0.0 13.9 1.0 S1 A:FES1499 2.2 14.4 1.0 S2 A:FES1499 2.2 14.8 1.0 SG A:CYS196 2.3 17.1 1.0 SG A:CYS403 2.4 15.1 1.0 FE2 A:FES1499 2.7 14.3 1.0 CB A:CYS403 3.3 14.4 1.0 CB A:CYS196 3.4 15.3 1.0 N A:CYS403 3.9 14.5 1.0 O A:HOH1690 3.9 26.8 1.0 CA A:CYS403 4.2 14.4 1.0 O A:HOH1649 4.4 17.5 1.0 CD A:ARG272 4.4 25.8 1.0 CB A:CYS406 4.4 17.9 1.0 SG A:CYS406 4.6 17.8 1.0 SG A:CYS411 4.6 18.0 1.0 CA A:CYS196 4.7 14.5 1.0 O A:HOH1731 4.9 18.9 1.0 NH1 A:ARG272 4.9 29.8 1.0

Iron binding site 2 out of 4 in the Crystal Structure of Human Ferrochelatase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Human Ferrochelatase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1499 b:14.3 occ:1.00 FE2 A:FES1499 0.0 14.3 1.0 S1 A:FES1499 2.2 14.4 1.0 S2 A:FES1499 2.2 14.8 1.0 SG A:CYS406 2.4 17.8 1.0 SG A:CYS411 2.4 18.0 1.0 FE1 A:FES1499 2.7 13.9 1.0 CB A:CYS411 3.2 17.3 1.0 CB A:CYS406 3.2 17.9 1.0 O A:HOH1690 4.2 26.8 1.0 O A:HOH1536 4.2 16.4 1.0 O A:HOH1731 4.2 18.9 1.0 CA A:CYS406 4.2 18.0 1.0 O A:ASN408 4.5 19.8 1.0 CB A:ASN408 4.5 20.2 1.0 SG A:CYS196 4.6 17.1 1.0 CA A:CYS411 4.6 17.4 1.0 SG A:CYS403 4.7 15.1 1.0 N A:CYS403 4.8 14.5 1.0 CB A:CYS403 4.8 14.4 1.0 CB A:CYS196 4.9 15.3 1.0 N A:ASN408 4.9 20.4 1.0 CB A:SER402 4.9 16.3 1.0 C A:CYS406 5.0 18.8 1.0 O A:HOH1664 5.0 26.6 1.0

Iron binding site 3 out of 4 in the Crystal Structure of Human Ferrochelatase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of Human Ferrochelatase within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe2999 b:14.7 occ:1.00 FE1 B:FES2999 0.0 14.7 1.0 S1 B:FES2999 2.2 15.2 1.0 S2 B:FES2999 2.3 15.6 1.0 SG B:CYS403 2.4 14.9 1.0 SG B:CYS196 2.4 17.4 1.0 FE2 B:FES2999 2.7 15.3 1.0 CB B:CYS403 3.3 14.8 1.0 CB B:CYS196 3.4 15.8 1.0 NH1 B:ARG272 3.8 30.0 1.0 N B:CYS403 3.9 15.1 1.0 O B:HOH3280 4.0 36.2 1.0 CA B:CYS403 4.2 14.9 1.0 O B:HOH3147 4.3 18.9 1.0 CB B:CYS406 4.5 16.6 1.0 CZ B:ARG272 4.5 29.2 1.0 SG B:CYS406 4.6 16.5 1.0 SG B:CYS411 4.6 17.5 1.0 CA B:CYS196 4.8 15.1 1.0 O B:HOH3243 5.0 29.7 1.0

Iron binding site 4 out of 4 in the Crystal Structure of Human Ferrochelatase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of Human Ferrochelatase within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe2999 b:15.3 occ:1.00 FE2 B:FES2999 0.0 15.3 1.0 S1 B:FES2999 2.2 15.2 1.0 S2 B:FES2999 2.2 15.6 1.0 SG B:CYS406 2.4 16.5 1.0 SG B:CYS411 2.4 17.5 1.0 FE1 B:FES2999 2.7 14.7 1.0 CB B:CYS411 3.2 17.3 1.0 CB B:CYS406 3.2 16.6 1.0 CA B:CYS406 4.2 16.8 1.0 O B:HOH3280 4.3 36.2 1.0 O B:HOH3084 4.3 22.1 1.0 O B:HOH3243 4.3 29.7 1.0 O B:ASN408 4.5 20.2 1.0 CB B:ASN408 4.5 20.9 1.0 SG B:CYS196 4.6 17.4 1.0 CA B:CYS411 4.6 17.4 1.0 SG B:CYS403 4.7 14.9 1.0 N B:CYS403 4.7 15.1 1.0 CB B:CYS403 4.7 14.8 1.0 N B:ASN408 4.9 20.1 1.0 CB B:CYS196 4.9 15.8 1.0 CB B:SER402 4.9 17.1 1.0 C B:CYS406 5.0 17.3 1.0

C.K.Wu, H.A.Dailey, J.P.Rose, A.Burden, V.M.Sellers, B.C.Wang. The 2.0 A Structure of Human Ferrochelatase, the Terminal Enzyme of Heme Biosynthesis. Nat.Struct.Biol. V. 8 156 2001.
ISSN: ISSN 1072-8368
PubMed: 11175906
DOI: 10.1038/84152