28wu

Crystal Structure of Catalase HPII (KatE) from Escherichia coli

Method: X-RAY DIFFRACTION D_max: 134.7 Å Quality: GOOD

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1. Protein Identity and Related Structures Protein Identity & Related Structures

Catalase HPII

OrganismNot specified

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 1–753 Chain B； UniProt 1–753 Chain C； UniProt 1–753 Chain D； UniProt 1–753	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7.75；293 K；0.1M Bis-Tris-Propane pH 7.75, 0.2M Na-acetate, 20% PEG3350.	Resolution 2.50 Å R-free 0.224

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 28WU	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1CF9 Structure of the mutant VAL169CYS of catalase HPII from Escherichia coli Deposited 1999-03-24	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 27–753（727 aa） Chain B 27–753（727 aa） Chain C 27–753（727 aa） Chain D 27–753（727 aa）	Mutation：V169C Mutation：V169C Mutation：V169C Mutation：V169C	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 9；pH 9	Resolution 1.80 Å R-free 0.237
1GG9 CRYSTAL STRUCTURE OF CATALASE HPII FROM ESCHERICHIA COLI, HIS128ASN VARIANT. Deposited 2000-08-11	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：H128N Mutation：H128N Mutation：H128N Mutation：H128N	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；297 K；PEG 3350, LiCl, Tris-HCl, pH 9.0, vapor diffusion/hanging drop, temperature 297.0K	Resolution 1.89 Å R-free 0.188
1GGE CRYSTAL STRUCTURE OF CATALASE HPII FROM ESCHERICHIA COLI, NATIVE STRUCTURE AT 1.9 A RESOLUTION. Deposited 2000-08-16	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Not recorded	HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；297 K；PEG 3350, LiCl, Tris-HCl, pH 9.00, VAPOR DIFFUSION, HANGING DROP, temperature 297.0K	Resolution 1.89 Å R-free 0.202
1GGF CRYSTAL STRUCTURE OF CATALASE HPII FROM ESCHERICHIA COLI, VARIANT HIS128ASN, COMPLEX WITH HYDROGEN PEROXIDE. Deposited 2000-08-21	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：H128N Mutation：H128N Mutation：H128N Mutation：H128N	HEM PROTOPORPHYRIN IX CONTAINING FE × 4 PEO HYDROGEN PEROXIDE × 13	X-RAY DIFFRACTION X-ray crystallization conditions pH 9；297 K；PEG 3350, LiCl, Tris-HCl. Before data collection the protein crystal was soaked during a few seconds in the solution with 2M hydrogen peroxide., pH 9.0, temperature 297.0K	Resolution 2.28 Å R-free 0.254
1GGH CRYSTAL STRUCTURE OF CATALASE HPII FROM ESCHERICHIA COLI, HIS128ALA VARIANT. Deposited 2000-08-21	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：H128A Mutation：H128A Mutation：H128A Mutation：H128A	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；297 K；PEG 3350, LiCl, Tris-HCl, pH 9.0, vapor diffusion/hanging drop, temperature 297.0K	Resolution 2.15 Å R-free 0.206
1GGJ CRYSTAL STRUCTURE OF CATALASE HPII FROM ESCHERICHIA COLI, ASN201ALA VARIANT. Deposited 2000-08-21	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：N201A Mutation：N201A Mutation：N201A Mutation：N201A	HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；297 K；PEG 3350, LiCl, Tris-HCl, pH 9.0, vapor diffusion/hanging drop, temperature 297.0K	Resolution 1.92 Å R-free 0.235
1GGK CRYSTAL STRUCTURE OF CATALASE HPII FROM ESCHERICHIA COLI, ASN201HIS VARIANT. Deposited 2000-08-21	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：N201H Mutation：N201H Mutation：N201H Mutation：N201H	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；297 K；PEG 3350, LiCl, Tris-HCl, pH 9.0, vapor diffusion/hanging drop, temperature 297.0K	Resolution 2.26 Å R-free 0.208
1IPH STRUCTURE OF CATALASE HPII FROM ESCHERICHIA COLI Deposited 1995-12-31	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å
1P7Y Crystal structure of the D181A variant of catalase HPII from E. coli Deposited 2003-05-06	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：D181A Mutation：D181A Mutation：D181A Mutation：D181A	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；295 K；PEG 3350, LiCl, Tris, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K	Resolution 2.40 Å R-free 0.225
1P7Z Crystal structure of the D181S variant of catalase HPII from E. coli Deposited 2003-05-06	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：D181S Mutation：D181S Mutation：D181S Mutation：D181S	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；295 K；PEG 3350, LiCl, Tris, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K	Resolution 2.21 Å R-free 0.211
1P80 Crystal structure of the D181Q variant of catalase HPII from E. coli Deposited 2003-05-06	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：D181Q Mutation：D181Q Mutation：D181Q Mutation：D181Q	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；298 K；PEG 3350, LiCl, Tris, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 1.65 Å R-free 0.202
1P81 Crystal structure of the D181E variant of catalase HPII from E. coli Deposited 2003-05-06	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：D181E Mutation：D181E Mutation：D181E Mutation：D181E	HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；295 K；PEG 3350, LiCl, Tris, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 295.0K	Resolution 1.81 Å R-free 0.216
1QF7 STRUCTURE OF THE MUTANT HIS392GLN OF CATALASE HPII FROM E. COLI Deposited 1999-03-26	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：H392Q Mutation：H392Q Mutation：H392Q Mutation：H392Q	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 9；pH 9	Resolution 2.20 Å R-free 0.210
1QWS Structure of the D181N variant of catalase HPII from E. coli Deposited 2003-09-03	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：D181N Mutation：D181N Mutation：D181N Mutation：D181N	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；15% PEG 3350, 1.6M LiCl, 0.1M Tris, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.90 Å R-free 0.220
1YE9 Crystal structure of proteolytically truncated catalase HPII from E. coli Deposited 2004-12-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain A 75–300（226 aa） Fragment：proteolytic fragment, residues 75-300 Chain B 75–300（226 aa） Fragment：proteolytic fragment, residues 75-300 Chain C 75–300（226 aa） Fragment：proteolytic fragment, residues 75-300 Chain D 75–300（226 aa） Fragment：proteolytic fragment, residues 75-300 Chain E 309–567（259 aa） Fragment：proteolytic fragment, residues 309-567 Chain F 309–567（259 aa） Fragment：proteolytic fragment, residues 309-567 Chain G 309–567（259 aa） Fragment：proteolytic fragment, residues 309-567 Chain H 309–567（259 aa） Fragment：proteolytic fragment, residues 309-567	Not recorded	HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；50mM TrisHCl, 8% PEG 20000, 8% PEG MME 550, 0.2M KSCN, 0.1M dithiothreitol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.80 Å R-free 0.269
1YE9 Crystal structure of proteolytically truncated catalase HPII from E. coli Deposited 2004-12-28	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric	Chain I 75–300（226 aa） Fragment：proteolytic fragment, residues 75-300 Chain J 75–300（226 aa） Fragment：proteolytic fragment, residues 75-300 Chain K 75–300（226 aa） Fragment：proteolytic fragment, residues 75-300 Chain L 75–300（226 aa） Fragment：proteolytic fragment, residues 75-300 Chain M 309–567（259 aa） Fragment：proteolytic fragment, residues 309-567 Chain N 309–567（259 aa） Fragment：proteolytic fragment, residues 309-567 Chain O 309–567（259 aa） Fragment：proteolytic fragment, residues 309-567 Chain P 309–567（259 aa） Fragment：proteolytic fragment, residues 309-567	Not recorded	HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；50mM TrisHCl, 8% PEG 20000, 8% PEG MME 550, 0.2M KSCN, 0.1M dithiothreitol, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.80 Å R-free 0.269
3P9P Structure of I274V variant of E. coli KatE Deposited 2010-10-18	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：I274V Mutation：I274V Mutation：I274V Mutation：I274V	HEM PROTOPORPHYRIN IX CONTAINING FE × 8 HDE CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE 17R, 18S × 4 HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；17% PEG3350, 1.6 M LiCl, 0.1 M Tris, pH 9.0, vapor diffusion, hanging drop, temperature 293K	Resolution 1.50 Å R-free 0.185
3P9Q Structure of I274C variant of E. coli KatE Deposited 2010-10-18	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：I274C Mutation：I274C Mutation：I274C Mutation：I274C	HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4 HDE CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE 17R, 18S × 4 H2S HYDROSULFURIC ACID × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；17% PEG3350, 1.6 M LiCl, 0.1 M Tris, pH 9.0, vapor diffusion, hanging drop, temperature 293K	Resolution 1.48 Å R-free 0.177
3P9R Structure of I274G variant of E. coli KatE Deposited 2010-10-18	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：I274G Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：I274G Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：I274G Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：I274G Non-standard monomer：Yes (specific site not provided by mmCIF)	HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；17% PEG3350, 1.6 M LiCl, 0.1 M Tris, pH 9.0, vapor diffusion, hanging drop, temperature 293K	Resolution 1.90 Å R-free 0.184
3P9S Structure of I274A variant of E. coli KatE Deposited 2010-10-18	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：I274A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：I274A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：I274A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：I274A Non-standard monomer：Yes (specific site not provided by mmCIF)	HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4 HDE CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE 17R, 18S × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；17% PEG3350, 1.6 M LiCl, 0.1 M Tris, pH 9.0, vapor diffusion, hanging drop, temperature 293K	Resolution 1.90 Å R-free 0.191
3PQ2 Structure of I274C variant of E. coli KatE[] - Images 1-6 Deposited 2010-11-25	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：I274C Mutation：I274C Mutation：I274C Mutation：I274C	HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4 HDE CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE 17R, 18S × 4 H2S HYDROSULFURIC ACID × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；17% PEG3350, 1.6 M LiCl, 0.1 M Tris, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.79 Å R-free 0.189
3PQ3 Structure of I274C variant of E. coli KatE[] - Images 7-12 Deposited 2010-11-25	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：I274C Mutation：I274C Mutation：I274C Mutation：I274C	HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4 HDE CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE 17R, 18S × 4 H2S HYDROSULFURIC ACID × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；17% PEG3350, 1.6 M LiCl, 0.1 M Tris, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.79 Å R-free 0.189
3PQ4 Structure of I274C variant of E. coli KatE[] - Images 13-18 Deposited 2010-11-25	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：I274C Mutation：I274C Mutation：I274C Mutation：I274C	HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4 HDE CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE 17R, 18S × 4 H2S HYDROSULFURIC ACID × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；17% PEG3350, 1.6 M LiCl, 0.1 M Tris, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.79 Å R-free 0.189
3PQ5 Structure of I274C variant of E. coli KatE[] - Images 19-24 Deposited 2010-11-25	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：I274C Mutation：I274C Mutation：I274C Mutation：I274C	HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4 HDE CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE 17R, 18S × 4 H2S HYDROSULFURIC ACID × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；17% PEG3350, 1.6 M LiCl, 0.1 M Tris, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.80 Å R-free 0.190
3PQ6 Structure of I274C variant of E. coli KatE[] - Images 25-30 Deposited 2010-11-25	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：I274C Mutation：I274C Mutation：I274C Mutation：I274C	HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4 HDE CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE 17R, 18S × 4 H2S HYDROSULFURIC ACID × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；17% PEG3350, 1.6 M LiCl, 0.1 M Tris, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.80 Å R-free 0.191
3PQ7 Structure of I274C variant of E. coli KatE[] - Images 31-36 Deposited 2010-11-25	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：I274C Mutation：I274C Mutation：I274C Mutation：I274C	HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4 HDE CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE 17R, 18S × 4 H2S HYDROSULFURIC ACID × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；17% PEG3350, 1.6 M LiCl, 0.1 M Tris, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.80 Å R-free 0.190
3PQ8 Structure of I274C variant of E. coli KatE[] - Images 37-42 Deposited 2010-11-25	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：I274C Mutation：I274C Mutation：I274C Mutation：I274C	HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4 HDE CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE 17R, 18S × 4 H2S HYDROSULFURIC ACID × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；17% PEG3350, 1.6 M LiCl, 0.1 M Tris, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.80 Å R-free 0.190
3TTT Structure of F413Y variant of E. coli KatE Deposited 2011-09-15	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：F413Y Mutation：F413Y Mutation：F413Y Mutation：F413Y	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；17% PEG3350, 1.6 M lithium chloride, 0.1 M Tris, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.58 Å R-free 0.189
3TTU Structure of F413Y/H128N double variant of E. coli KatE Deposited 2011-09-15	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：F413Y/H128N Mutation：F413Y/H128N Mutation：F413Y/H128N Mutation：F413Y/H128N	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；17% PEG3350, 1.6 M lithium chloride, 0.1 M Tris, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.89 Å R-free 0.193
3TTV Structure of the F413E variant of E. coli KatE Deposited 2011-09-15	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：F413Y/T115A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：F413Y/T115A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：F413Y/T115A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：F413Y/T115A Non-standard monomer：Yes (specific site not provided by mmCIF)	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；17% PEG3350, 1.6 M lithium chloride, 0.1 M Tris, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.45 Å R-free 0.172
3TTW Structure of the F413E variant of E. coli KatE Deposited 2011-09-15	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：F413E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：F413E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：F413E Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：F413E Non-standard monomer：Yes (specific site not provided by mmCIF)	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；17% PEG3350, 1.6 M lithium chloride, 0.1 M Tris, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.62 Å R-free 0.199
3TTX Structure of the F413K variant of E. coli KatE Deposited 2011-09-15	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：F413K Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：F413K Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：F413K Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：F413K Non-standard monomer：Yes (specific site not provided by mmCIF)	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；17% PEG3350, 1.6 M lithium chloride, 0.1 M Tris, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.74 Å R-free 0.185
3VU3 Crystal structure of the Hfq and catalase HPII complex Deposited 2012-06-15	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 28 PDB declaration: 28-meric	Chain A 1–753（753 aa）	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；0.1M Tris-HCl, 0.18M NaCl, 10% PEG4000, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.85 Å R-free 0.246
4BFL Structure of natively expressed catalase HPII Deposited 2013-03-19	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4 EDO 1,2-ETHANEDIOL × 3	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.5；10 % PEG 20000, 20% PEG 500MME, 30 MM SODIUM NITRATE, 30 MM DISODIUM HYDROGENPHOSPHATE, 30 MM AMMONIUM SULFATE, AND 100 MM MES/IMIDAZOLE PH 6.5	Resolution 1.64 Å R-free 0.202
4ENP Structure of E530A variant E. coli KatE Deposited 2012-04-13	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：E530A Mutation：E530A Mutation：E530A Mutation：E530A	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；17% PEG3350, 1.6 M LiCl, 0.1 M Tris, pH 9.0, vapor diffusion, hanging drop, temperature 293K	Resolution 1.50 Å R-free 0.162
4ENQ Structure of E530D variant E. coli KatE Deposited 2012-04-13	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：E530D Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：E530D Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：E530D Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：E530D Non-standard monomer：Yes (specific site not provided by mmCIF)	HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；17% PEG3350, 1.6 M LiCl, 0.1 M Tris, pH 9.0, vapor diffusion, hanging drop, temperature 293K	Resolution 1.90 Å R-free 0.207
4ENR Structure of E530I variant E. coli KatE Deposited 2012-04-13	Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：E530I Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：E530I Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：E530I Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：E530I Non-standard monomer：Yes (specific site not provided by mmCIF)	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；17% PEG3350, 1.6 M LiCl, 0.1 M Tris, pH 9.0, vapor diffusion, hanging drop, temperature 293K	Resolution 1.60 Å R-free 0.193
4ENS Structure of E530Q variant of E. coli KatE Deposited 2012-04-13	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：E530Q Mutation：E530Q Mutation：E530Q Mutation：E530Q	HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；17% PEG3350, 1.6 M LiCl, 0.1 M Tris, pH 9.0, vapor diffusion, hanging drop, temperature 293K	Resolution 1.60 Å R-free 0.184
4ENT Structure of the S234A variant of E. coli KatE Deposited 2012-04-13	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：S234A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：S234A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：S234A Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：S234A Non-standard monomer：Yes (specific site not provided by mmCIF)	HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；17% PEG3350, 1.6 M LiCl, 0.1 M Tris, pH 9.0, vapor diffusion, hanging drop, temperature 293K	Resolution 1.70 Å R-free 0.197
4ENU Structure of the S234D variant of E. coli KatE Deposited 2012-04-13	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：S234D Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：S234D Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：S234D Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：S234D Non-standard monomer：Yes (specific site not provided by mmCIF)	HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；17% PEG3350, 1.6 M LiCl, 0.1 M Tris, pH 9.0, vapor diffusion, hanging drop, temperature 293K	Resolution 1.70 Å R-free 0.170
4ENV Structure of the S234I variant of E. coli KatE Deposited 2012-04-13	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：S234I Mutation：S234I Mutation：S234I Mutation：S234I	HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；17% PEG3350, 1.6 M LiCl, 0.1 M Tris, pH 9.0, vapor diffusion, hanging drop, temperature 293K	Resolution 1.70 Å R-free 0.207
4ENW Structure of the S234N variant of E. coli KatE Deposited 2012-04-13	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：S234N Mutation：S234N Mutation：S234N Mutation：S234N	HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9；293 K；17% PEG3350, 1.6 M LiCl, 0.1 M Tris, pH 9.0, vapor diffusion, hanging drop, temperature 293K	Resolution 1.90 Å R-free 0.221
5BV2 Crystal structure of E. coli HPII catalase variant Deposited 2015-06-04	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain P 1–753（753 aa） Chain Q 1–753（753 aa） Chain R 1–753（753 aa） Chain S 1–753（753 aa）	Not recorded	HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4 GOL GLYCEROL × 11 EDO 1,2-ETHANEDIOL × 39 PGE TRIETHYLENE GLYCOL × 3 PEG DI(HYDROXYETHYL)ETHER × 10 SO4 SULFATE ION × 2 MG MAGNESIUM ION × 2 PG4 TETRAETHYLENE GLYCOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；2% PEG20000, 15% PEG5000 MME, 0.1 M potassium chloride, 0.1 M manganese acetate, 0.1 M HEPES	Resolution 1.53 Å R-free 0.132
6BY0 Crystal structure of catalase HPII from E. coli in space group P1 Deposited 2017-12-19	Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；292 K；0.085 M sodium HEPES pH 7.5, 17% w/v PEG 4000, 15% v/v glycerol, 8.5% v/v isopropanol or 0.1 M HEPES pH 7.0, 20% w/v PEG 6000, 1.0 M lithium chloride	Resolution 2.93 Å R-free 0.236
6ZTV Crystal Structure of catalase HPII from Escherichia coli (serendipitously crystallized) Deposited 2020-07-20	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：S99N Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：S99N Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：S99N Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：S99N Non-standard monomer：Yes (specific site not provided by mmCIF)	HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4 GOL GLYCEROL × 1 EDO 1,2-ETHANEDIOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；292 K；0.2 M NaCl, 0.1 M Tris pH 7.5, 20% w/v PEG 4000, 10% MPD	Resolution 1.78 Å R-free 0.229
6ZTW Crystal Structure of catalase HPII from Escherichia coli (serendipitously crystallized) Deposited 2020-07-20	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：S99N Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：S99N Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：S99N Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：S99N Non-standard monomer：Yes (specific site not provided by mmCIF)	HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 4 GOL GLYCEROL × 4 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 EDO 1,2-ETHANEDIOL × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；292 K；0.1 M Tris pH 7.5, 20% w/v PEG 4000	Resolution 1.84 Å R-free 0.184
6ZTW Crystal Structure of catalase HPII from Escherichia coli (serendipitously crystallized) Deposited 2020-07-20	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain E 1–753（753 aa） Chain F 1–753（753 aa） Chain G 1–753（753 aa） Chain H 1–753（753 aa）	Mutation：S99N Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：S99N Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：S99N Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：S99N Non-standard monomer：Yes (specific site not provided by mmCIF)	HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 5 GOL GLYCEROL × 2 EDO 1,2-ETHANEDIOL × 3	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；292 K；0.1 M Tris pH 7.5, 20% w/v PEG 4000	Resolution 1.84 Å R-free 0.184
6ZTX Crystal Structure of catalase HPII from Escherichia coli (serendipitously crystallized) Deposited 2020-07-20	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–753（753 aa） Chain B 1–753（753 aa） Chain C 1–753（753 aa） Chain D 1–753（753 aa）	Mutation：R37S, S99D, K372N, R521S Mutation：R37S, S99D, K372N, R521S Mutation：R37S, S99D, K372N, R521S Mutation：R37S, S99D, K372N, R521S	GOL GLYCEROL × 4 EDO 1,2-ETHANEDIOL × 7 HDD CIS-HEME D HYDROXYCHLORIN GAMMA-SPIROLACTONE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；292 K；0.2 M lithium sulfate monohydrate, 0.1 M Tris pH 8.5, 25% w/v polyethylene glycol 3350	Resolution 1.30 Å R-free 0.162

46 other PDB entries and 48 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CATE_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–753； UniProt 1–753 Author chain B； PDBConstruct 1–753； UniProt 1–753 Author chain C； PDBConstruct 1–753； UniProt 1–753 Author chain D； PDBConstruct 1–753； UniProt 1–753

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	28wu
Deposition date deposition_date	2026-02-25
最后修订 last_revision	2026-05-06
Structure title title	Crystal Structure of Catalase HPII (KatE) from Escherichia coli
Keywords keywords	Calatase HPII, KatE, hydrogen-peroxide, heme, iron-protein, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	41.75 Å
Radius of gyration Rg (electron density) rg_electron	41.46 Å
Forward intensity I(0) i0	1551810000.00
Molecular weight molecular_weight	326700.0 kDa
Excluded volume excluded_volume	408220 Å³
Envelope volume envelope_volume	482140 Å³
Hydration-shell volume shell_volume	90470 Å³
Envelope diameter envelope_diameter	145.0 Å
Shell Rg shell_rg	50.74 Å
Envelope Rg envelope_rg	41.88 Å
Shape Rg shape_rg	41.40 Å
Total Rg total_rg	42.05 Å
Total atoms total_atoms	23116
Residues n_residues	2903
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	134.7 Å
Rg (real space) rg_real	41.67 Å
Rg uncertainty (real space) rg_real_error	0.64 Å
I(0) (real space) i0_real	1.5520e+09
I(0) uncertainty (real space) i0_real_error	2.3920e+07
Rg (reciprocal space) rg_reciprocal	41.75 Å
I(0) (reciprocal space) i0_reciprocal	1552000000.0000
Solution quality estimate total_estimate	0.8725
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	49.6 Å
Skewness Skewness skewness	0.369
Kurtosis Kurtosis kurtosis	-0.181
Angular range angular_range	— – 0.1900 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	643500000.0000
Real-space data points n_real_points	39
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.847; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.978; Smooth: 0.820

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	Catalase HPII
Molecular weight formula_weight	84271.5 kDa
EC 编号 ec_number	1.11.1.6
Source method src_method	nat
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	24169

MSQHNEKNPHQHQSPLHDSSEAKPGMDSLAPEDGSHRPAAEPTPPGAQPTAPGSLKAPDTRNEKLNSLEDVRKGSENYALTTNQGVRIADDQNSLRAGSRGPTLLEDFILREKITHFDHERIPERIVHARGSAAHGYFQPYKSLSDITKADFLSDPNKITPVFVRFSTVQGGAGSADTVRDIRGFATKFYTEEGIFDLVGNNTPIFFIQDAHKFPDFVHAVKPEPHWAIPQGQSAHDTFWDYVSLQPETLHNVMWAMSDRGIPRSYRTMEGFGIHTFRLINAEGKATFVRFHWKPLAGKASLVWDEAQKLTGRDPDFHRRELWEAIEAGDFPEYELGFQLIPEEDEFKFDFDLLDPTKLIPEELVPVQRVGKMVLNRNPDNFFAENEQAAFHPGHIVPGLDFTNDPLLQGRLFSYTDTQISRLGGPNFHEIPINRPTCPYHNFQRDGMHRMGIDTNPANYEPNSINDNWPRETPPGPKRGGFESYQERVEGNKVRERSPSFGEYYSHPRLFWLSQTPFEQRHIVDGFSFELSKVVRPYIRERVVDQLAHIDLTLAQAVAKNLGIELTDDQLNITPPPDVNGLKKDPSLSLYAIPDGDVKGRVVAILLNDEVRSADLLAILKALKAKGVHAKLLYSRMGEVTADDGTVLPIAATFAGAPSLTVDAVIVPCGNIADIADNGDANYYLMEAYKHLKPIALAGDARKFKATIKIADQGEEGIVEADSADGSFMDELLTLMAAHRVWSRIPKIDKIPA

Entity 2 Entity 2 non-polymer

Description description	PROTOPORPHYRIN IX CONTAINING FE
Molecular weight formula_weight	616.5 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1053

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8. Citations (1)

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Unit-cell length a length_a	93.664 Å
Unit-cell length b length_b	136.795 Å
Unit-cell length c length_c	122.299 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	112.42 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.500 Å
Low-resolution limit resolution_low	41.235 Å
R factor r_factor	0.1597
R_work r_work	0.1562
R_free r_free	0.2236

fit	/app/data/saxs_computation/8w/28wu/28wu.fit
pddf	/app/data/pr_computation/8w/28wu/28wu.pr.out
profile	/app/data/saxs_computation/8w/28wu/28wu.dat