Bromine 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:

Iron

(Fe)

4 atoms

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

Bromine 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 Bromine with other atoms in the Br binding site number 1 of Human Erythrocyte Catalse Complexed with Bt-Br within 5.0Å range: probe atom residue distance (Å) B Occ A:Br601 b:97.3 occ:1.00 BR7 A:LLR601 0.0 97.3 1.0 C05 A:LLR601 1.9 59.6 1.0 OH A:TYR215 2.7 32.2 1.0 C06 A:LLR601 2.9 58.7 1.0 C04 A:LLR601 2.9 63.6 1.0 N14 A:LLR601 3.1 63.7 1.0 CZ A:TYR215 3.4 30.7 1.0 CE2 A:PHE198 3.4 41.7 1.0 C15 A:LLR601 3.5 58.1 1.0 CD A:PRO151 3.5 34.0 1.0 C18 A:LLR601 3.7 51.9 1.0 NH1 A:ARG203 3.9 41.7 1.0 C16 A:LLR601 3.9 53.1 1.0 CG A:PRO151 3.9 32.5 1.0 C17 A:LLR601 3.9 50.6 1.0 CZ A:PHE198 4.0 35.8 1.0 CE2 A:TYR215 4.0 28.4 1.0 CE1 A:TYR215 4.1 24.9 1.0 C01 A:LLR601 4.2 55.6 1.0 C03 A:LLR601 4.2 57.8 1.0 CD2 A:PHE198 4.4 46.4 1.0 CZ A:ARG203 4.6 43.2 1.0 C02 A:LLR601 4.7 59.1 1.0 NH2 A:ARG203 4.8 33.5 1.0 N A:PRO151 4.9 27.8 1.0

Bromine 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 Bromine with other atoms in the Br binding site number 2 of Human Erythrocyte Catalse Complexed with Bt-Br within 5.0Å range: probe atom residue distance (Å) B Occ B:Br601 b:102.4 occ:1.00 BR7 B:LLR601 0.0 102.4 1.0 C05 B:LLR601 1.9 62.2 1.0 C04 B:LLR601 2.9 60.2 1.0 C06 B:LLR601 2.9 54.9 1.0 N14 B:LLR601 3.1 59.3 1.0 OH B:TYR215 3.1 29.1 1.0 C17 B:LLR601 3.5 55.1 1.0 CZ B:TYR215 3.7 29.6 1.0 CD B:PRO151 3.7 29.6 1.0 C15 B:LLR601 3.7 53.3 1.0 CG B:PRO151 3.8 36.8 1.0 CE1 B:PHE198 4.1 48.2 1.0 C03 B:LLR601 4.2 60.1 1.0 C01 B:LLR601 4.2 60.0 1.0 NH1 B:ARG203 4.2 32.7 1.0 CE2 B:TYR215 4.3 32.0 1.0 O B:HOH1092 4.3 49.8 1.0 CE1 B:TYR215 4.4 32.3 1.0 NH2 B:ARG203 4.4 40.7 1.0 CZ B:PHE198 4.4 46.2 1.0 CZ B:ARG203 4.7 40.2 1.0 C02 B:LLR601 4.7 59.4 1.0 C18 B:LLR601 4.8 59.7 1.0 CD1 B:PHE198 4.9 48.0 1.0 C16 B:LLR601 4.9 43.6 1.0 CB B:PRO151 4.9 31.4 1.0

Bromine 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 Bromine with other atoms in the Br binding site number 3 of Human Erythrocyte Catalse Complexed with Bt-Br within 5.0Å range: probe atom residue distance (Å) B Occ C:Br601 b:108.4 occ:1.00 BR7 C:LLR601 0.0 108.4 1.0 C05 C:LLR601 1.9 71.0 1.0 C04 C:LLR601 2.9 73.8 1.0 C06 C:LLR601 2.9 64.6 1.0 OH C:TYR215 3.1 38.7 1.0 N14 C:LLR601 3.1 69.8 1.0 CE1 C:PHE198 3.6 49.8 1.0 CD C:PRO151 3.6 35.6 1.0 C17 C:LLR601 3.7 64.4 1.0 C15 C:LLR601 3.7 60.9 1.0 CZ C:TYR215 3.8 40.4 1.0 C16 C:LLR601 3.8 58.4 1.0 CG C:PRO151 3.8 39.0 1.0 CZ C:PHE198 3.9 36.0 1.0 C01 C:LLR601 4.2 63.8 1.0 C03 C:LLR601 4.2 72.4 1.0 CE2 C:TYR215 4.4 42.0 1.0 CE1 C:TYR215 4.4 32.3 1.0 NH2 C:ARG203 4.5 37.8 1.0 CD1 C:PHE198 4.6 34.4 1.0 C02 C:LLR601 4.7 70.6 1.0 NH1 C:ARG203 4.8 50.4 1.0 CZ C:ARG203 5.0 41.0 1.0 CB C:PRO151 5.0 34.4 1.0

Bromine 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 Bromine with other atoms in the Br binding site number 4 of Human Erythrocyte Catalse Complexed with Bt-Br within 5.0Å range: probe atom residue distance (Å) B Occ D:Br601 b:105.1 occ:1.00 BR7 D:LLR601 0.0 105.1 1.0 C05 D:LLR601 1.9 74.7 1.0 C04 D:LLR601 2.9 75.8 1.0 C06 D:LLR601 2.9 66.6 1.0 OH D:TYR215 3.0 46.9 1.0 N14 D:LLR601 3.1 71.9 1.0 C15 D:LLR601 3.5 68.4 1.0 C18 D:LLR601 3.5 65.6 1.0 CZ D:TYR215 3.7 35.6 1.0 NH1 D:ARG203 3.9 54.6 1.0 CD D:PRO151 3.9 27.4 1.0 C17 D:LLR601 3.9 60.9 1.0 NH2 D:ARG203 4.0 58.8 1.0 CG D:PRO151 4.1 30.2 1.0 CE1 D:PHE198 4.2 41.2 1.0 C01 D:LLR601 4.2 73.8 1.0 C03 D:LLR601 4.2 73.3 1.0 CZ D:ARG203 4.3 66.7 1.0 CE2 D:TYR215 4.4 35.8 1.0 CE1 D:TYR215 4.4 34.4 1.0 CZ D:PHE198 4.5 38.2 1.0 C02 D:LLR601 4.7 74.8 1.0 CD1 D:PHE198 4.9 48.8 1.0 C16 D:LLR601 5.0 63.7 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