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1p81

Crystal structure of the D181E variant of catalase HPII from E. coli

Method: X-RAY DIFFRACTION Dmax: 134.4 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Catalase HPII

Escherichia coli

UniProt P21179

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 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

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 1P81 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 ligand/ion 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 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 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 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）
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 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：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 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 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：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 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）
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 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：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 ligand/ion 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 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：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
1QF7 STRUCTURE OF THE MUTANT HIS392GLN OF CATALASE HPII FROM E. COLI Deposited 1999-03-26 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：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 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：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 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 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
28WU Crystal Structure of Catalase HPII (KatE) from Escherichia coli Deposited 2026-02-25 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）
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
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 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 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：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 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：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 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：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 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：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 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：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 ligand/ion 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 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）
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 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：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 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 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：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 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 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 mutation/modification 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 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）
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

SAXS profile for 1p81

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1p81
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1p81
Deposition date deposition_date2003-05-06
Structure title titleCrystal structure of the D181E variant of catalase HPII from E. coli
Keywords keywordscatalase, beta barrel, channel, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier41.65 Å
Radius of gyration Rg (electron density) rg_electron41.37 Å
Forward intensity I(0) i01561190000.00
Molecular weight molecular_weight327400.0 kDa
Excluded volume excluded_volume408960 ų
Envelope volume envelope_volume480290 ų
Hydration-shell volume shell_volume90250 ų
Envelope diameter envelope_diameter146.3 Å
Shell Rg shell_rg50.71 Å
Envelope Rg envelope_rg41.81 Å
Shape Rg shape_rg41.30 Å
Total Rg total_rg41.95 Å
Total atoms total_atoms23164
Residues n_residues2908
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax134.4 Å
Rg (real space) rg_real41.57 Å
Rg uncertainty (real space) rg_real_error0.73 Å
I(0) (real space) i0_real1.5610e+09
I(0) uncertainty (real space) i0_real_error2.7010e+07
Rg (reciprocal space) rg_reciprocal41.64 Å
I(0) (reciprocal space) i0_reciprocal1561000000.0000
Solution quality estimate total_estimate0.8724
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary49.5 Å
Skewness Skewness skewness0.371
Kurtosis Kurtosis kurtosis-0.179
Angular range angular_range— – 0.1900 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha646400000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
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)

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7. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (8 domains)

Domain ID domain_idd1p81a1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.23 — Flavodoxin-like
Superfamily Superfamily superfamilyc.23.16 — Class I glutamine amidotransferase-like
Family Family familyc.23.16.3 — Catalase, C-terminal domain
Domain ID domain_idd1p81a2
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.5 — Heme-dependent catalase-like
Superfamily Superfamily superfamilye.5.1 — Heme-dependent catalase-like
Family Family familye.5.1.1 — Heme-dependent catalases
Domain ID domain_idd1p81b1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.23 — Flavodoxin-like
Superfamily Superfamily superfamilyc.23.16 — Class I glutamine amidotransferase-like
Family Family familyc.23.16.3 — Catalase, C-terminal domain
Domain ID domain_idd1p81b2
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.5 — Heme-dependent catalase-like
Superfamily Superfamily superfamilye.5.1 — Heme-dependent catalase-like
Family Family familye.5.1.1 — Heme-dependent catalases
Domain ID domain_idd1p81c1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.23 — Flavodoxin-like
Superfamily Superfamily superfamilyc.23.16 — Class I glutamine amidotransferase-like
Family Family familyc.23.16.3 — Catalase, C-terminal domain
Domain ID domain_idd1p81c2
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.5 — Heme-dependent catalase-like
Superfamily Superfamily superfamilye.5.1 — Heme-dependent catalase-like
Family Family familye.5.1.1 — Heme-dependent catalases
Domain ID domain_idd1p81d1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.23 — Flavodoxin-like
Superfamily Superfamily superfamilyc.23.16 — Class I glutamine amidotransferase-like
Family Family familyc.23.16.3 — Catalase, C-terminal domain
Domain ID domain_idd1p81d2
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.5 — Heme-dependent catalase-like
Superfamily Superfamily superfamilye.5.1 — Heme-dependent catalase-like
Family Family familye.5.1.1 — Heme-dependent catalases

CATH v4.4 (12 domains)

Domain ID domain_id1p81A01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology180 — Catalase HpII, Chain A, domain 1
Homologous superfamily homologous superfamily10 — Catalase core domain
Domain ID domain_id1p81A02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1370 — Hemocyanin, N-terminal domain
Homologous superfamily homologous superfamily20 — Catalase, four-helical domain
Domain ID domain_id1p81A03
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily880 — Class I glutamine amidotransferase (GATase) domain
Domain ID domain_id1p81B01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology180 — Catalase HpII, Chain A, domain 1
Homologous superfamily homologous superfamily10 — Catalase core domain
Domain ID domain_id1p81B02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1370 — Hemocyanin, N-terminal domain
Homologous superfamily homologous superfamily20 — Catalase, four-helical domain
Domain ID domain_id1p81B03
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily880 — Class I glutamine amidotransferase (GATase) domain
Domain ID domain_id1p81C01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology180 — Catalase HpII, Chain A, domain 1
Homologous superfamily homologous superfamily10 — Catalase core domain
Domain ID domain_id1p81C02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1370 — Hemocyanin, N-terminal domain
Homologous superfamily homologous superfamily20 — Catalase, four-helical domain
Domain ID domain_id1p81C03
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily880 — Class I glutamine amidotransferase (GATase) domain
Domain ID domain_id1p81D01
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology180 — Catalase HpII, Chain A, domain 1
Homologous superfamily homologous superfamily10 — Catalase core domain
Domain ID domain_id1p81D02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology1370 — Hemocyanin, N-terminal domain
Homologous superfamily homologous superfamily20 — Catalase, four-helical domain
Domain ID domain_id1p81D03
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily880 — Class I glutamine amidotransferase (GATase) domain
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8. Citations (1)

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9. Files and Curves (10)