Iron in PDB 28wu: Crystal Structure of Catalase Hpii (Kate) From Escherichia Coli

All present enzymatic activity of Crystal Structure of Catalase Hpii (Kate) From Escherichia Coli:
1.11.1.6;

The structure of Crystal Structure of Catalase Hpii (Kate) From Escherichia Coli, PDB code: 28wu was solved by R.Schnell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.24 / 2.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	93.664, 136.795, 122.299, 90, 112.42, 90
R / Rfree (%)	15.6 / 22.4

The binding sites of Iron atom in the Crystal Structure of Catalase Hpii (Kate) From Escherichia Coli (pdb code 28wu). 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 Catalase Hpii (Kate) From Escherichia Coli, PDB code: 28wu:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystal Structure of Catalase Hpii (Kate) From Escherichia Coli


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 Catalase Hpii (Kate) From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:11.2 occ:1.00 FE A:HEM801 0.0 11.2 1.0 ND A:HEM801 2.0 9.0 1.0 NC A:HEM801 2.0 9.2 1.0 NA A:HEM801 2.1 14.3 1.0 NB A:HEM801 2.1 11.6 1.0 OH A:TYR415 2.1 35.4 1.0 C4C A:HEM801 3.0 10.0 1.0 C4D A:HEM801 3.0 9.6 1.0 C1D A:HEM801 3.0 9.8 1.0 C1C A:HEM801 3.0 9.9 1.0 C1A A:HEM801 3.0 13.8 1.0 CZ A:TYR415 3.1 12.3 1.0 C4B A:HEM801 3.1 11.6 1.0 C4A A:HEM801 3.1 12.4 1.0 C1B A:HEM801 3.2 13.0 1.0 CHD A:HEM801 3.4 9.9 1.0 CHA A:HEM801 3.4 13.6 1.0 CHC A:HEM801 3.4 11.8 1.0 CHB A:HEM801 3.6 12.2 1.0 CE1 A:TYR415 3.8 11.2 1.0 CE2 A:TYR415 3.8 9.3 1.0 NE A:ARG411 4.1 10.6 1.0 C3C A:HEM801 4.1 11.6 1.0 C2C A:HEM801 4.2 15.8 1.0 C3D A:HEM801 4.2 11.9 1.0 C2D A:HEM801 4.2 11.2 1.0 C2A A:HEM801 4.3 12.2 1.0 C3B A:HEM801 4.3 13.8 1.0 C3A A:HEM801 4.3 14.8 1.0 NH2 A:ARG411 4.3 12.0 1.0 C2B A:HEM801 4.3 11.6 1.0 O A:HOH1052 4.5 12.9 1.0 CZ A:ARG411 4.6 12.1 1.0 CG2 A:VAL127 4.7 10.5 1.0 NE2 A:HIS128 4.7 10.4 1.0 CZ A:PHE214 4.7 9.4 1.0 CD2 A:HIS128 4.8 10.9 1.0 CD A:ARG411 5.0 12.3 1.0

Iron binding site 2 out of 4 in the Crystal Structure of Catalase Hpii (Kate) From Escherichia Coli


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 Catalase Hpii (Kate) From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe801 b:18.3 occ:1.00 FE B:HEM801 0.0 18.3 1.0 OH B:TYR415 1.9 11.8 1.0 ND B:HEM801 2.0 10.9 1.0 NA B:HEM801 2.0 15.0 1.0 NC B:HEM801 2.0 15.7 1.0 NB B:HEM801 2.1 15.0 1.0 CZ B:TYR415 3.0 16.8 1.0 C4C B:HEM801 3.0 16.9 1.0 C1D B:HEM801 3.0 13.3 1.0 C4A B:HEM801 3.0 14.8 1.0 C1A B:HEM801 3.0 16.2 1.0 C4D B:HEM801 3.0 13.3 1.0 C1C B:HEM801 3.1 19.4 1.0 C1B B:HEM801 3.1 18.4 1.0 C4B B:HEM801 3.1 13.7 1.0 CHD B:HEM801 3.3 16.1 1.0 CHA B:HEM801 3.4 12.6 1.0 CHB B:HEM801 3.4 16.6 1.0 CHC B:HEM801 3.5 13.2 1.0 CE2 B:TYR415 3.7 16.5 1.0 CE1 B:TYR415 3.9 16.4 1.0 C3C B:HEM801 4.2 16.8 1.0 C2D B:HEM801 4.2 14.2 1.0 C3D B:HEM801 4.2 15.5 1.0 C3A B:HEM801 4.2 16.4 1.0 C2A B:HEM801 4.3 19.7 1.0 C2C B:HEM801 4.3 16.8 1.0 NE B:ARG411 4.3 17.2 1.0 C3B B:HEM801 4.3 17.1 1.0 C2B B:HEM801 4.3 18.9 1.0 NH2 B:ARG411 4.4 17.1 1.0 NE2 B:HIS128 4.5 17.9 1.0 CG2 B:VAL127 4.6 13.8 1.0 O B:HOH979 4.6 16.1 1.0 CD2 B:HIS128 4.6 14.3 1.0 CZ B:ARG411 4.7 17.6 1.0 CZ B:PHE214 4.8 13.7 1.0 CD2 B:TYR415 4.9 17.3 1.0

Iron binding site 3 out of 4 in the Crystal Structure of Catalase Hpii (Kate) From Escherichia Coli


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 Catalase Hpii (Kate) From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe801 b:11.8 occ:1.00 FE C:HEM801 0.0 11.8 1.0 NB C:HEM801 2.0 12.3 1.0 NC C:HEM801 2.0 13.1 1.0 OH C:TYR415 2.0 11.5 1.0 NA C:HEM801 2.1 11.7 1.0 ND C:HEM801 2.1 13.4 1.0 C4B C:HEM801 3.0 14.1 1.0 CZ C:TYR415 3.0 12.1 1.0 C1C C:HEM801 3.0 14.1 1.0 C1B C:HEM801 3.0 13.2 1.0 C4D C:HEM801 3.1 14.6 1.0 C4C C:HEM801 3.1 12.6 1.0 C1A C:HEM801 3.1 12.0 1.0 C4A C:HEM801 3.1 11.9 1.0 C1D C:HEM801 3.1 12.4 1.0 CHC C:HEM801 3.3 14.0 1.0 CHB C:HEM801 3.4 12.0 1.0 CHA C:HEM801 3.5 13.4 1.0 CHD C:HEM801 3.5 10.5 1.0 CE2 C:TYR415 3.5 12.4 1.0 CE1 C:TYR415 3.9 14.2 1.0 NE C:ARG411 4.1 14.1 1.0 C3B C:HEM801 4.2 16.5 1.0 NH2 C:ARG411 4.2 11.6 1.0 C2C C:HEM801 4.2 10.6 1.0 C2B C:HEM801 4.2 14.7 1.0 C3C C:HEM801 4.3 12.2 1.0 C2A C:HEM801 4.3 10.0 1.0 C3D C:HEM801 4.3 16.2 1.0 C3A C:HEM801 4.3 10.8 1.0 C2D C:HEM801 4.3 15.5 1.0 O C:HOH1036 4.5 13.6 1.0 CZ C:ARG411 4.5 14.8 1.0 CZ C:PHE214 4.7 13.2 1.0 CG2 C:VAL127 4.7 11.4 1.0 CD2 C:TYR415 4.8 11.7 1.0 NE2 C:HIS128 4.8 13.4 1.0 CD2 C:HIS128 4.9 13.4 1.0

Iron binding site 4 out of 4 in the Crystal Structure of Catalase Hpii (Kate) From Escherichia Coli


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 Catalase Hpii (Kate) From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe801 b:11.8 occ:1.00 FE D:HEM801 0.0 11.8 1.0 ND D:HEM801 2.0 12.6 1.0 NC D:HEM801 2.0 14.7 1.0 NB D:HEM801 2.0 15.8 1.0 NA D:HEM801 2.0 14.1 1.0 OH D:TYR415 2.2 23.4 1.0 C4C D:HEM801 3.0 13.8 1.0 C4B D:HEM801 3.0 12.2 1.0 C1D D:HEM801 3.0 14.4 1.0 C1C D:HEM801 3.0 15.2 1.0 C1A D:HEM801 3.0 13.8 1.0 C4D D:HEM801 3.0 11.1 1.0 C4A D:HEM801 3.1 14.2 1.0 C1B D:HEM801 3.1 14.2 1.0 CZ D:TYR415 3.2 14.0 1.0 CHD D:HEM801 3.4 13.1 1.0 CHC D:HEM801 3.4 11.5 1.0 CHA D:HEM801 3.4 14.4 1.0 CHB D:HEM801 3.5 13.6 1.0 CE1 D:TYR415 4.0 14.2 1.0 CE2 D:TYR415 4.0 15.0 1.0 NE D:ARG411 4.1 14.1 1.0 C3C D:HEM801 4.2 15.7 1.0 C3B D:HEM801 4.2 16.4 1.0 NH2 D:ARG411 4.2 11.2 1.0 C2C D:HEM801 4.2 13.8 1.0 C2D D:HEM801 4.2 14.4 1.0 C3D D:HEM801 4.2 10.7 1.0 C2A D:HEM801 4.3 18.2 1.0 C3A D:HEM801 4.3 16.0 1.0 C2B D:HEM801 4.3 14.5 1.0 O D:HOH960 4.4 13.3 1.0 NE2 D:HIS128 4.6 11.6 1.0 CZ D:ARG411 4.6 15.2 1.0 CG2 D:VAL127 4.6 10.4 1.0 CD2 D:HIS128 4.7 14.7 1.0 CZ D:PHE214 4.7 14.2 1.0

A.T.Scholz, L.Coppo, E.Nolan, M.Hernandez, X.Wang, P.Mishra, R.Schnell, Z.A.Pato, Y.Chen, M.Dagnell, A.Andor, Q.Cheng, E.S.J.Arner. A Kate Katg Double-Knockout E. Coli Strain Eliminates the Risk of Catalase Contamination in Recombinant Proteins. Appl.Microbiol.Biotechnol. V. 110 2026.
ISSN: ESSN 1432-0614
PubMed: 42020871
DOI: 10.1007/S00253-026-13820-2