Iron in PDB 8hid: Human Erythrocyte Catalse Complexed with Bt-Br

All present enzymatic activity of Human Erythrocyte Catalse Complexed with Bt-Br:
1.11.1.6;

The structure of Human Erythrocyte Catalse Complexed with Bt-Br, PDB code: 8hid was solved by H.-Y.Lin, G.-F.Yang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.57 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	83.466, 140.871, 233.428, 90, 90, 90
R / Rfree (%)	22.5 / 26.5

The structure of Human Erythrocyte Catalse Complexed with Bt-Br also contains other interesting chemical elements:

Bromine

(Br)

4 atoms

The binding sites of Iron atom in the Human Erythrocyte Catalse Complexed with Bt-Br (pdb code 8hid). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Human Erythrocyte Catalse Complexed with Bt-Br, PDB code: 8hid:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Human Erythrocyte Catalse Complexed with Bt-Br


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Human Erythrocyte Catalse Complexed with Bt-Br within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe602 b:42.4 occ:1.00 FE A:HEM602 0.0 42.4 1.0 ND A:HEM602 2.0 25.7 1.0 NC A:HEM602 2.1 24.6 1.0 NA A:HEM602 2.1 28.5 1.0 NB A:HEM602 2.1 26.0 1.0 OH A:TYR358 2.4 22.3 1.0 C1C A:HEM602 3.0 25.8 1.0 C4D A:HEM602 3.0 29.2 1.0 C1A A:HEM602 3.1 27.1 1.0 C4B A:HEM602 3.1 27.2 1.0 C4C A:HEM602 3.1 25.1 1.0 C1D A:HEM602 3.1 22.2 1.0 C1B A:HEM602 3.1 24.9 1.0 C4A A:HEM602 3.1 29.1 1.0 CHC A:HEM602 3.4 23.0 1.0 CHA A:HEM602 3.4 22.7 1.0 CZ A:TYR358 3.4 23.3 1.0 CHD A:HEM602 3.4 21.9 1.0 CHB A:HEM602 3.5 24.6 1.0 CE2 A:TYR358 4.0 22.1 1.0 O A:HOH985 4.1 26.7 1.0 C2C A:HEM602 4.2 23.6 1.0 C3C A:HEM602 4.3 26.1 1.0 C3D A:HEM602 4.3 24.4 1.0 C2D A:HEM602 4.3 25.0 1.0 C2A A:HEM602 4.3 25.1 1.0 C3B A:HEM602 4.3 27.2 1.0 C2B A:HEM602 4.3 24.4 1.0 C3A A:HEM602 4.3 19.1 1.0 CG2 A:VAL74 4.3 20.7 1.0 NH2 A:ARG354 4.3 21.7 1.0 NE A:ARG354 4.4 20.7 1.0 CE1 A:TYR358 4.4 26.6 1.0 CZ A:PHE161 4.4 27.3 1.0 CD2 A:HIS75 4.5 24.8 1.0 NE2 A:HIS75 4.6 25.5 1.0 CZ A:ARG354 4.8 23.3 1.0

Iron binding site 2 out of 4 in the Human Erythrocyte Catalse Complexed with Bt-Br


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Human Erythrocyte Catalse Complexed with Bt-Br within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe602 b:37.6 occ:1.00 FE B:HEM602 0.0 37.6 1.0 NB B:HEM602 2.0 26.2 1.0 NC B:HEM602 2.1 31.1 1.0 NA B:HEM602 2.1 25.2 1.0 ND B:HEM602 2.1 23.4 1.0 OH B:TYR358 2.4 23.8 1.0 C4C B:HEM602 3.0 30.8 1.0 C4B B:HEM602 3.0 25.6 1.0 C1B B:HEM602 3.1 24.2 1.0 C1C B:HEM602 3.1 29.5 1.0 C4A B:HEM602 3.1 22.3 1.0 C1D B:HEM602 3.1 24.6 1.0 C1A B:HEM602 3.1 27.0 1.0 C4D B:HEM602 3.1 23.8 1.0 CHC B:HEM602 3.4 22.9 1.0 CHD B:HEM602 3.4 27.4 1.0 CHB B:HEM602 3.4 24.6 1.0 CZ B:TYR358 3.4 24.0 1.0 CHA B:HEM602 3.4 24.6 1.0 O B:HOH904 3.9 31.1 1.0 CE2 B:TYR358 4.1 25.1 1.0 C3C B:HEM602 4.2 26.9 1.0 C2C B:HEM602 4.3 26.9 1.0 C3B B:HEM602 4.3 25.5 1.0 C2B B:HEM602 4.3 25.8 1.0 CE1 B:TYR358 4.3 22.1 1.0 C3A B:HEM602 4.3 22.4 1.0 C2D B:HEM602 4.3 27.9 1.0 C2A B:HEM602 4.3 25.2 1.0 C3D B:HEM602 4.3 28.2 1.0 CZ B:PHE161 4.3 22.3 1.0 NH2 B:ARG354 4.3 24.7 1.0 NE B:ARG354 4.4 25.7 1.0 NE2 B:HIS75 4.4 29.4 1.0 CG2 B:VAL74 4.6 29.2 1.0 CD2 B:HIS75 4.6 20.4 1.0 CZ B:ARG354 4.7 25.2 1.0 CE1 B:PHE161 4.9 20.6 1.0 CE2 B:PHE161 4.9 18.6 1.0

Iron binding site 3 out of 4 in the Human Erythrocyte Catalse Complexed with Bt-Br


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Human Erythrocyte Catalse Complexed with Bt-Br within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe602 b:42.2 occ:1.00 FE C:HEM602 0.0 42.2 1.0 NB C:HEM602 2.0 25.0 1.0 NC C:HEM602 2.0 25.1 1.0 ND C:HEM602 2.1 27.8 1.0 NA C:HEM602 2.1 24.6 1.0 OH C:TYR358 2.4 27.9 1.0 C1B C:HEM602 3.0 24.5 1.0 C4C C:HEM602 3.1 29.2 1.0 C1D C:HEM602 3.1 27.0 1.0 C4B C:HEM602 3.1 21.7 1.0 C4A C:HEM602 3.1 23.1 1.0 C1C C:HEM602 3.1 22.0 1.0 C4D C:HEM602 3.1 25.5 1.0 C1A C:HEM602 3.1 25.2 1.0 CZ C:TYR358 3.4 20.6 1.0 CHD C:HEM602 3.4 28.1 1.0 CHB C:HEM602 3.4 21.1 1.0 CHC C:HEM602 3.4 22.8 1.0 CHA C:HEM602 3.5 28.2 1.0 CE2 C:TYR358 4.0 23.1 1.0 O C:HOH739 4.1 26.0 1.0 CE1 C:TYR358 4.2 26.5 1.0 C2B C:HEM602 4.3 28.2 1.0 C3C C:HEM602 4.3 27.1 1.0 C2D C:HEM602 4.3 25.8 1.0 C3B C:HEM602 4.3 20.7 1.0 C2C C:HEM602 4.3 23.6 1.0 C3A C:HEM602 4.3 30.8 1.0 C3D C:HEM602 4.3 21.6 1.0 C2A C:HEM602 4.3 25.0 1.0 NE C:ARG354 4.3 22.5 1.0 NH2 C:ARG354 4.4 22.4 1.0 CZ C:PHE161 4.4 22.8 1.0 CG2 C:VAL74 4.5 26.1 1.0 CD2 C:HIS75 4.5 19.7 1.0 NE2 C:HIS75 4.5 27.2 1.0 CZ C:ARG354 4.7 25.3 1.0 CE1 C:PHE161 4.9 19.9 1.0

Iron binding site 4 out of 4 in the Human Erythrocyte Catalse Complexed with Bt-Br


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Human Erythrocyte Catalse Complexed with Bt-Br within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe602 b:43.7 occ:1.00 FE D:HEM602 0.0 43.7 1.0 ND D:HEM602 2.0 24.5 1.0 NB D:HEM602 2.0 26.3 1.0 NA D:HEM602 2.1 22.8 1.0 NC D:HEM602 2.1 30.3 1.0 OH D:TYR358 2.4 26.6 1.0 C4B D:HEM602 3.1 26.9 1.0 C1C D:HEM602 3.1 28.2 1.0 C1B D:HEM602 3.1 24.0 1.0 C4A D:HEM602 3.1 19.7 1.0 C4D D:HEM602 3.1 30.6 1.0 C1D D:HEM602 3.1 26.1 1.0 C4C D:HEM602 3.1 32.9 1.0 C1A D:HEM602 3.1 21.5 1.0 CHC D:HEM602 3.4 26.8 1.0 CHB D:HEM602 3.4 28.2 1.0 CZ D:TYR358 3.4 23.3 1.0 CHA D:HEM602 3.4 25.6 1.0 CHD D:HEM602 3.4 28.5 1.0 O D:HOH712 3.9 36.2 1.0 CE2 D:TYR358 4.1 26.9 1.0 C2C D:HEM602 4.3 22.6 1.0 C2B D:HEM602 4.3 26.5 1.0 C3B D:HEM602 4.3 26.2 1.0 C2D D:HEM602 4.3 24.9 1.0 C3D D:HEM602 4.3 25.9 1.0 C3A D:HEM602 4.3 22.2 1.0 C3C D:HEM602 4.3 31.5 1.0 NE D:ARG354 4.3 23.7 1.0 C2A D:HEM602 4.3 20.6 1.0 CE1 D:TYR358 4.3 26.0 1.0 CZ D:PHE161 4.4 22.9 1.0 NH2 D:ARG354 4.5 25.6 1.0 CD2 D:HIS75 4.5 26.1 1.0 NE2 D:HIS75 4.6 32.0 1.0 CG2 D:VAL74 4.6 21.5 1.0 CZ D:ARG354 4.7 30.6 1.0 CE1 D:PHE161 4.9 23.7 1.0

Y.Y.Cao, Y.Y.Chen, M.S.Wang, J.J.Tong, M.Xu, C.Zhao, H.Y.Lin, L.C.Mei, J.Dong, W.L.Zhang, Y.X.Qin, W.Huang, D.Zhang, G.F.Yang. A Catalase Inhibitor: Targeting the Nadph-Binding Site For Castration-Resistant Prostate Cancer Therapy. Redox Biol V. 63 02751 2023.
ISSN: ISSN 2213-2317
PubMed: 37216701
DOI: 10.1016/J.REDOX.2023.102751