Iron in PDB 2po5: Crystal Structure of Human Ferrochelatase Mutant with His 263 Replaced By Cys

All present enzymatic activity of Crystal Structure of Human Ferrochelatase Mutant with His 263 Replaced By Cys:
4.99.1.1;

The structure of Crystal Structure of Human Ferrochelatase Mutant with His 263 Replaced By Cys, PDB code: 2po5 was solved by H.A.Dailey, C.-K.Wu, P.Horanyi, A.E.Medlock, A.E.W.Najahi-Missaoui, A.Burden, T.A.Dailey, J.P.Rose, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.90 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	93.420, 87.730, 109.580, 90.00, 90.00, 90.00
R / Rfree (%)	20.9 / 24

The binding sites of Iron atom in the Crystal Structure of Human Ferrochelatase Mutant with His 263 Replaced By Cys (pdb code 2po5). 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 Mutant with His 263 Replaced By Cys, PDB code: 2po5:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystal Structure of Human Ferrochelatase Mutant with His 263 Replaced By Cys


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 Mutant with His 263 Replaced By Cys within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe499 b:26.5 occ:1.00 FE1 A:FES499 0.0 26.5 1.0 S1 A:FES499 2.2 19.9 1.0 S2 A:FES499 2.3 21.5 1.0 SG A:CYS406 2.4 23.5 1.0 SG A:CYS411 2.5 26.9 1.0 FE2 A:FES499 2.7 23.9 1.0 CB A:CYS406 3.1 25.3 1.0 CB A:CYS411 3.2 22.8 1.0 O A:HOH643 3.9 43.3 1.0 O A:HOH516 4.1 26.4 1.0 CA A:CYS406 4.1 24.1 1.0 CB A:ASN408 4.4 26.8 1.0 O A:ASN408 4.5 25.6 1.0 SG A:CYS196 4.6 23.4 1.0 SG A:CYS403 4.7 21.1 1.0 CA A:CYS411 4.7 22.6 1.0 CB A:CYS403 4.8 18.9 1.0 N A:CYS403 4.8 19.2 1.0 N A:ASN408 4.9 29.3 1.0 CB A:CYS196 4.9 20.8 1.0 C A:CYS406 5.0 25.5 1.0

Iron binding site 2 out of 4 in the Crystal Structure of Human Ferrochelatase Mutant with His 263 Replaced By Cys


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 Mutant with His 263 Replaced By Cys within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe499 b:23.9 occ:1.00 FE2 A:FES499 0.0 23.9 1.0 S1 A:FES499 2.2 19.9 1.0 S2 A:FES499 2.3 21.5 1.0 SG A:CYS196 2.3 23.4 1.0 SG A:CYS403 2.4 21.1 1.0 FE1 A:FES499 2.7 26.5 1.0 CB A:CYS403 3.3 18.9 1.0 CB A:CYS196 3.4 20.8 1.0 O A:HOH643 3.6 43.3 1.0 NH1 A:ARG272 3.6 42.0 1.0 N A:CYS403 3.9 19.2 1.0 CA A:CYS403 4.2 20.1 1.0 O A:HOH618 4.2 31.4 1.0 CB A:CYS406 4.5 25.3 1.0 CZ A:ARG272 4.6 39.9 1.0 SG A:CYS411 4.7 26.9 1.0 SG A:CYS406 4.7 23.5 1.0 CA A:CYS196 4.7 19.4 1.0

Iron binding site 3 out of 4 in the Crystal Structure of Human Ferrochelatase Mutant with His 263 Replaced By Cys


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 Mutant with His 263 Replaced By Cys within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe999 b:23.6 occ:1.00 FE1 B:FES999 0.0 23.6 1.0 S1 B:FES999 2.2 19.1 1.0 S2 B:FES999 2.3 23.3 1.0 SG B:CYS403 2.3 20.0 1.0 SG B:CYS196 2.3 24.6 1.0 FE2 B:FES999 2.7 22.2 1.0 CB B:CYS403 3.3 19.9 1.0 CB B:CYS196 3.4 20.2 1.0 NH1 B:ARG272 3.6 40.8 1.0 O B:HOH1146 3.9 40.2 1.0 N B:CYS403 3.9 20.0 1.0 O B:HOH1104 4.2 28.3 1.0 CA B:CYS403 4.2 19.7 1.0 CB B:CYS406 4.5 24.3 1.0 CZ B:ARG272 4.5 38.1 1.0 SG B:CYS411 4.7 25.8 1.0 SG B:CYS406 4.7 24.2 1.0 CA B:CYS196 4.7 19.1 1.0

Iron binding site 4 out of 4 in the Crystal Structure of Human Ferrochelatase Mutant with His 263 Replaced By Cys


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 Mutant with His 263 Replaced By Cys within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe999 b:22.2 occ:1.00 FE2 B:FES999 0.0 22.2 1.0 S1 B:FES999 2.2 19.1 1.0 S2 B:FES999 2.2 23.3 1.0 SG B:CYS406 2.4 24.2 1.0 SG B:CYS411 2.4 25.8 1.0 FE1 B:FES999 2.7 23.6 1.0 CB B:CYS406 3.2 24.3 1.0 CB B:CYS411 3.2 21.9 1.0 O B:HOH1146 4.0 40.2 1.0 CA B:CYS406 4.2 24.3 1.0 O B:HOH1017 4.2 28.5 1.0 O B:HOH1125 4.4 43.6 1.0 CB B:ASN408 4.5 28.6 1.0 O B:ASN408 4.5 26.5 1.0 SG B:CYS196 4.6 24.6 1.0 SG B:CYS403 4.7 20.0 1.0 CA B:CYS411 4.7 21.8 1.0 CB B:CYS403 4.8 19.9 1.0 N B:CYS403 4.8 20.0 1.0 CB B:CYS196 4.9 20.2 1.0 N B:ASN408 4.9 29.8 1.0 C B:CYS406 5.0 24.8 1.0

H.A.Dailey, C.-K.Wu, P.Horanyi, A.E.Medlock, W.Najahi-Missaoui, A.E.Burden, T.A.Dailey, J.P.Rose. Altered Orientation of Active Site Residues in Variants of Human Ferrochelatase. Evidence For A Hydrogen Bond Network Involved in Catalysis Biochemistry V. 46 7973 2007.
ISSN: ISSN 0006-2960
PubMed: 17567154
DOI: 10.1021/BI700151F