Iron in PDB 8wzk: Human Erythrocyte Catalase

All present enzymatic activity of Human Erythrocyte Catalase:
1.11.1.6;

The binding sites of Iron atom in the Human Erythrocyte Catalase (pdb code 8wzk). 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 Catalase, PDB code: 8wzk:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Human Erythrocyte Catalase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Human Erythrocyte Catalase within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe3001 b:70.1 occ:1.00 FE B:HEM3001 0.0 70.1 1.0 OH B:TYR358 1.9 76.3 1.0 ND B:HEM3001 1.9 69.9 1.0 NA B:HEM3001 2.0 76.5 1.0 NB B:HEM3001 2.1 71.2 1.0 NC B:HEM3001 2.1 71.6 1.0 C4D B:HEM3001 2.9 73.3 1.0 C1D B:HEM3001 2.9 73.7 1.0 C1A B:HEM3001 3.0 72.7 1.0 CZ B:TYR358 3.0 91.8 1.0 C4A B:HEM3001 3.0 80.0 1.0 C1B B:HEM3001 3.0 81.2 1.0 C4B B:HEM3001 3.0 79.5 1.0 C4C B:HEM3001 3.1 67.0 1.0 C1C B:HEM3001 3.2 69.0 1.0 CHA B:HEM3001 3.3 76.1 1.0 CHD B:HEM3001 3.4 74.5 1.0 CHB B:HEM3001 3.4 76.3 1.0 CHC B:HEM3001 3.5 79.5 1.0 CE1 B:TYR358 3.8 90.3 1.0 CE2 B:TYR358 3.9 95.7 1.0 NH2 B:ARG354 4.1 72.9 1.0 C3D B:HEM3001 4.2 75.7 1.0 C2A B:HEM3001 4.2 76.9 1.0 C2D B:HEM3001 4.2 67.7 1.0 NE B:ARG354 4.2 71.7 1.0 C3A B:HEM3001 4.2 76.5 1.0 C2B B:HEM3001 4.2 83.4 1.0 C3B B:HEM3001 4.3 92.2 1.0 C3C B:HEM3001 4.4 77.7 1.0 C2C B:HEM3001 4.4 81.5 1.0 CZ B:PHE161 4.4 81.9 1.0 CZ B:ARG354 4.5 75.1 1.0 CG2 B:VAL74 4.6 72.4 1.0

Iron binding site 2 out of 4 in the Human Erythrocyte Catalase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Human Erythrocyte Catalase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe3001 b:70.2 occ:1.00 FE A:HEM3001 0.0 70.2 1.0 ND A:HEM3001 1.9 70.3 1.0 OH A:TYR358 1.9 73.8 1.0 NA A:HEM3001 2.0 76.6 1.0 NB A:HEM3001 2.1 71.2 1.0 NC A:HEM3001 2.1 71.8 1.0 C4D A:HEM3001 2.9 73.6 1.0 C1D A:HEM3001 2.9 74.1 1.0 C1A A:HEM3001 3.0 72.6 1.0 CZ A:TYR358 3.0 92.5 1.0 C4A A:HEM3001 3.0 79.9 1.0 C1B A:HEM3001 3.0 81.3 1.0 C4B A:HEM3001 3.0 79.5 1.0 C4C A:HEM3001 3.1 67.0 1.0 C1C A:HEM3001 3.2 69.0 1.0 CHA A:HEM3001 3.3 75.9 1.0 CHD A:HEM3001 3.4 74.5 1.0 CHB A:HEM3001 3.4 76.4 1.0 CHC A:HEM3001 3.5 79.5 1.0 CE1 A:TYR358 3.8 90.0 1.0 CE2 A:TYR358 3.9 96.0 1.0 NH2 A:ARG354 4.1 72.7 1.0 C3D A:HEM3001 4.2 75.7 1.0 C2A A:HEM3001 4.2 76.8 1.0 C2D A:HEM3001 4.2 67.6 1.0 NE A:ARG354 4.2 71.5 1.0 C3A A:HEM3001 4.2 76.5 1.0 C2B A:HEM3001 4.2 83.4 1.0 C3B A:HEM3001 4.3 92.2 1.0 C3C A:HEM3001 4.4 77.7 1.0 C2C A:HEM3001 4.4 81.6 1.0 CZ A:PHE161 4.4 81.8 1.0 CZ A:ARG354 4.5 74.9 1.0 CG2 A:VAL74 4.6 72.4 1.0

Iron binding site 3 out of 4 in the Human Erythrocyte Catalase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Human Erythrocyte Catalase within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe3001 b:70.2 occ:1.00 FE C:HEM3001 0.0 70.2 1.0 ND C:HEM3001 1.9 70.3 1.0 OH C:TYR358 1.9 73.8 1.0 NA C:HEM3001 2.0 76.7 1.0 NB C:HEM3001 2.1 71.3 1.0 NC C:HEM3001 2.1 71.8 1.0 C4D C:HEM3001 2.9 73.6 1.0 C1D C:HEM3001 2.9 74.1 1.0 C1A C:HEM3001 3.0 72.6 1.0 CZ C:TYR358 3.0 92.6 1.0 C4A C:HEM3001 3.0 79.9 1.0 C1B C:HEM3001 3.0 81.3 1.0 C4B C:HEM3001 3.0 79.6 1.0 C4C C:HEM3001 3.1 67.0 1.0 C1C C:HEM3001 3.2 68.9 1.0 CHA C:HEM3001 3.3 75.9 1.0 CHD C:HEM3001 3.4 74.5 1.0 CHB C:HEM3001 3.4 76.3 1.0 CHC C:HEM3001 3.5 79.6 1.0 CE1 C:TYR358 3.8 90.0 1.0 CE2 C:TYR358 3.9 96.0 1.0 NH2 C:ARG354 4.1 72.7 1.0 C3D C:HEM3001 4.2 75.7 1.0 C2A C:HEM3001 4.2 76.9 1.0 C2D C:HEM3001 4.2 67.6 1.0 NE C:ARG354 4.2 71.4 1.0 C3A C:HEM3001 4.2 76.5 1.0 C2B C:HEM3001 4.2 83.4 1.0 C3B C:HEM3001 4.3 92.3 1.0 C3C C:HEM3001 4.4 77.7 1.0 C2C C:HEM3001 4.4 81.5 1.0 CZ C:PHE161 4.4 81.8 1.0 CZ C:ARG354 4.5 74.9 1.0 CG2 C:VAL74 4.6 72.4 1.0

Iron binding site 4 out of 4 in the Human Erythrocyte Catalase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Human Erythrocyte Catalase within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe3001 b:70.2 occ:1.00 FE D:HEM3001 0.0 70.2 1.0 ND D:HEM3001 1.9 70.3 1.0 OH D:TYR358 1.9 73.8 1.0 NA D:HEM3001 2.0 76.6 1.0 NB D:HEM3001 2.1 71.2 1.0 NC D:HEM3001 2.1 71.7 1.0 C4D D:HEM3001 2.9 73.6 1.0 C1D D:HEM3001 2.9 74.1 1.0 C1A D:HEM3001 3.0 72.6 1.0 CZ D:TYR358 3.0 92.6 1.0 C4A D:HEM3001 3.0 79.9 1.0 C1B D:HEM3001 3.0 81.3 1.0 C4B D:HEM3001 3.0 79.7 1.0 C4C D:HEM3001 3.1 67.0 1.0 C1C D:HEM3001 3.2 68.9 1.0 CHA D:HEM3001 3.4 75.9 1.0 CHD D:HEM3001 3.4 74.5 1.0 CHB D:HEM3001 3.4 76.3 1.0 CHC D:HEM3001 3.5 79.6 1.0 CE1 D:TYR358 3.8 90.1 1.0 CE2 D:TYR358 3.9 96.1 1.0 NH2 D:ARG354 4.1 72.6 1.0 C3D D:HEM3001 4.2 75.7 1.0 C2A D:HEM3001 4.2 76.8 1.0 C2D D:HEM3001 4.2 67.7 1.0 NE D:ARG354 4.2 71.4 1.0 C3A D:HEM3001 4.2 76.5 1.0 C2B D:HEM3001 4.2 83.4 1.0 C3B D:HEM3001 4.3 92.2 1.0 C3C D:HEM3001 4.4 77.7 1.0 C2C D:HEM3001 4.4 81.6 1.0 CZ D:PHE161 4.4 81.8 1.0 CZ D:ARG354 4.5 74.9 1.0 CG2 D:VAL74 4.6 72.4 1.0

S.Yadav, K.R.Vinothkumar. Factors Affecting Macromolecule Orientations in Thin Films Formed in Cryo-Em. Acta Crystallogr D Struct 2024BIOL.
ISSN: ISSN 2059-7983
PubMed: 38935342
DOI: 10.1107/S2059798324005229