Iron in PDB 8wzm: Human Erythrocyte Catalase with Ctab As Additive During Em Sample Preparation

All present enzymatic activity of Human Erythrocyte Catalase with Ctab As Additive During Em Sample Preparation:
1.11.1.6;

The binding sites of Iron atom in the Human Erythrocyte Catalase with Ctab As Additive During Em Sample Preparation (pdb code 8wzm). 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 with Ctab As Additive During Em Sample Preparation, PDB code: 8wzm:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Human Erythrocyte Catalase with Ctab As Additive During Em Sample Preparation


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 with Ctab As Additive During Em Sample Preparation within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe3001 b:81.3 occ:1.00 FE B:HEM3001 0.0 81.3 1.0 OH B:TYR358 1.9 81.3 1.0 ND B:HEM3001 2.0 81.3 1.0 NA B:HEM3001 2.0 81.3 1.0 NB B:HEM3001 2.0 81.3 1.0 NC B:HEM3001 2.1 81.3 1.0 C1C B:HEM3001 3.0 81.3 1.0 C4B B:HEM3001 3.0 81.3 1.0 C4C B:HEM3001 3.0 81.3 1.0 CZ B:TYR358 3.1 81.3 1.0 C4D B:HEM3001 3.1 81.3 1.0 C1D B:HEM3001 3.1 81.3 1.0 C1A B:HEM3001 3.1 81.3 1.0 C4A B:HEM3001 3.1 81.3 1.0 C1B B:HEM3001 3.1 81.3 1.0 CHC B:HEM3001 3.4 81.3 1.0 CHA B:HEM3001 3.4 81.3 1.0 CHD B:HEM3001 3.4 81.3 1.0 CHB B:HEM3001 3.4 81.3 1.0 CE1 B:TYR358 3.8 81.3 1.0 CE2 B:TYR358 3.9 81.3 1.0 NE B:ARG354 4.2 81.3 1.0 C2C B:HEM3001 4.2 81.3 1.0 C3C B:HEM3001 4.2 81.3 1.0 C3B B:HEM3001 4.3 81.3 1.0 C2B B:HEM3001 4.3 81.3 1.0 C2D B:HEM3001 4.3 81.3 1.0 C3A B:HEM3001 4.3 81.3 1.0 C3D B:HEM3001 4.3 81.3 1.0 C2A B:HEM3001 4.3 81.3 1.0 NH2 B:ARG354 4.3 81.3 1.0 CZ B:PHE161 4.4 81.3 1.0 CZ B:ARG354 4.6 81.3 1.0 CG2 B:VAL74 4.6 81.3 1.0 CD2 B:HIS75 4.9 81.3 1.0 CE1 B:PHE161 4.9 81.3 1.0 NE2 B:HIS75 4.9 81.3 1.0

Iron binding site 2 out of 4 in the Human Erythrocyte Catalase with Ctab As Additive During Em Sample Preparation


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 with Ctab As Additive During Em Sample Preparation within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe3001 b:81.3 occ:1.00 FE A:HEM3001 0.0 81.3 1.0 OH A:TYR358 1.9 81.3 1.0 ND A:HEM3001 2.0 81.3 1.0 NA A:HEM3001 2.0 81.3 1.0 NB A:HEM3001 2.0 81.3 1.0 NC A:HEM3001 2.1 81.3 1.0 C1C A:HEM3001 3.0 81.3 1.0 C4B A:HEM3001 3.0 81.3 1.0 C4C A:HEM3001 3.0 81.3 1.0 CZ A:TYR358 3.1 81.3 1.0 C4D A:HEM3001 3.1 81.3 1.0 C1A A:HEM3001 3.1 81.3 1.0 C1D A:HEM3001 3.1 81.3 1.0 C4A A:HEM3001 3.1 81.3 1.0 C1B A:HEM3001 3.1 81.3 1.0 CHC A:HEM3001 3.4 81.3 1.0 CHA A:HEM3001 3.4 81.3 1.0 CHD A:HEM3001 3.4 81.3 1.0 CHB A:HEM3001 3.4 81.3 1.0 CE1 A:TYR358 3.8 81.3 1.0 CE2 A:TYR358 3.9 81.3 1.0 NE A:ARG354 4.2 81.3 1.0 C2C A:HEM3001 4.2 81.3 1.0 C3C A:HEM3001 4.2 81.3 1.0 C3B A:HEM3001 4.3 81.3 1.0 C2B A:HEM3001 4.3 81.3 1.0 C3A A:HEM3001 4.3 81.3 1.0 C3D A:HEM3001 4.3 81.3 1.0 C2D A:HEM3001 4.3 81.3 1.0 C2A A:HEM3001 4.3 81.3 1.0 NH2 A:ARG354 4.3 81.3 1.0 CZ A:PHE161 4.4 81.3 1.0 CZ A:ARG354 4.6 81.3 1.0 CG2 A:VAL74 4.6 81.3 1.0 CD2 A:HIS75 4.9 81.3 1.0 CE1 A:PHE161 4.9 81.3 1.0 NE2 A:HIS75 4.9 81.3 1.0

Iron binding site 3 out of 4 in the Human Erythrocyte Catalase with Ctab As Additive During Em Sample Preparation


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 with Ctab As Additive During Em Sample Preparation within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe3001 b:81.3 occ:1.00 FE C:HEM3001 0.0 81.3 1.0 OH C:TYR358 1.9 81.3 1.0 ND C:HEM3001 2.0 81.3 1.0 NA C:HEM3001 2.0 81.3 1.0 NB C:HEM3001 2.0 81.3 1.0 NC C:HEM3001 2.1 81.3 1.0 C1C C:HEM3001 3.0 81.3 1.0 C4B C:HEM3001 3.0 81.3 1.0 C4C C:HEM3001 3.0 81.3 1.0 CZ C:TYR358 3.1 81.3 1.0 C4D C:HEM3001 3.1 81.3 1.0 C1D C:HEM3001 3.1 81.3 1.0 C1A C:HEM3001 3.1 81.3 1.0 C4A C:HEM3001 3.1 81.3 1.0 C1B C:HEM3001 3.1 81.3 1.0 CHC C:HEM3001 3.4 81.3 1.0 CHA C:HEM3001 3.4 81.3 1.0 CHD C:HEM3001 3.4 81.3 1.0 CHB C:HEM3001 3.4 81.3 1.0 CE1 C:TYR358 3.8 81.3 1.0 CE2 C:TYR358 3.9 81.3 1.0 NE C:ARG354 4.2 81.3 1.0 C2C C:HEM3001 4.2 81.3 1.0 C3C C:HEM3001 4.2 81.3 1.0 C3B C:HEM3001 4.3 81.3 1.0 C2B C:HEM3001 4.3 81.3 1.0 C2D C:HEM3001 4.3 81.3 1.0 C3D C:HEM3001 4.3 81.3 1.0 C3A C:HEM3001 4.3 81.3 1.0 C2A C:HEM3001 4.3 81.3 1.0 NH2 C:ARG354 4.3 81.3 1.0 CZ C:PHE161 4.4 81.3 1.0 CZ C:ARG354 4.6 81.3 1.0 CG2 C:VAL74 4.6 81.3 1.0 CD2 C:HIS75 4.9 81.3 1.0 CE1 C:PHE161 4.9 81.3 1.0 NE2 C:HIS75 4.9 81.3 1.0

Iron binding site 4 out of 4 in the Human Erythrocyte Catalase with Ctab As Additive During Em Sample Preparation


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 with Ctab As Additive During Em Sample Preparation within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe3001 b:81.3 occ:1.00 FE D:HEM3001 0.0 81.3 1.0 OH D:TYR358 1.9 81.3 1.0 ND D:HEM3001 2.0 81.3 1.0 NA D:HEM3001 2.0 81.3 1.0 NB D:HEM3001 2.0 81.3 1.0 NC D:HEM3001 2.1 81.3 1.0 C1C D:HEM3001 3.0 81.3 1.0 C4B D:HEM3001 3.0 81.3 1.0 C4C D:HEM3001 3.0 81.3 1.0 CZ D:TYR358 3.1 81.3 1.0 C4D D:HEM3001 3.1 81.3 1.0 C1D D:HEM3001 3.1 81.3 1.0 C1A D:HEM3001 3.1 81.3 1.0 C4A D:HEM3001 3.1 81.3 1.0 C1B D:HEM3001 3.1 81.3 1.0 CHC D:HEM3001 3.4 81.3 1.0 CHA D:HEM3001 3.4 81.3 1.0 CHD D:HEM3001 3.4 81.3 1.0 CHB D:HEM3001 3.4 81.3 1.0 CE1 D:TYR358 3.8 81.3 1.0 CE2 D:TYR358 3.9 81.3 1.0 NE D:ARG354 4.2 81.3 1.0 C2C D:HEM3001 4.2 81.3 1.0 C3C D:HEM3001 4.2 81.3 1.0 C3B D:HEM3001 4.3 81.3 1.0 C2B D:HEM3001 4.3 81.3 1.0 C3D D:HEM3001 4.3 81.3 1.0 C3A D:HEM3001 4.3 81.3 1.0 C2D D:HEM3001 4.3 81.3 1.0 C2A D:HEM3001 4.3 81.3 1.0 NH2 D:ARG354 4.3 81.3 1.0 CZ D:PHE161 4.4 81.3 1.0 CZ D:ARG354 4.6 81.3 1.0 CG2 D:VAL74 4.6 81.3 1.0 CD2 D:HIS75 4.9 81.3 1.0 CE1 D:PHE161 4.9 81.3 1.0 NE2 D:HIS75 4.9 81.3 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