1th4

crystal structure of NADPH depleted bovine liver catalase complexed with 3-amino-1,2,4-triazole

Method: X-RAY DIFFRACTION D_max: 110.1 Å Quality: GOOD

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

Catalase

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 1–506 Chain B； UniProt 1–506 Chain C； UniProt 1–506 Chain D； UniProt 1–506	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4 3TR 3-AMINO-1,2,4-TRIAZOLE × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.98 Å R-free 0.292

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 1TH4	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1TGU The crystal structure of bovine liver catalase without NADPH Deposited 2004-05-31	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–506（506 aa） Chain B 1–506（506 aa） Chain C 1–506（506 aa） Chain D 1–506（506 aa）	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；273 K；Tris Hcl buffer, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 273K	Resolution 2.80 Å R-free 0.249
1TH2 crystal structure of NADPH depleted bovine liver catalase complexed with azide Deposited 2004-06-01	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–506（506 aa） Chain B 1–506（506 aa） Chain C 1–506（506 aa） Chain D 1–506（506 aa）	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4 AZI AZIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.80 Å R-free 0.280
1TH3 Crystal structure of NADPH depleted bovine live catalase complexed with cyanide Deposited 2004-06-01	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–506（506 aa） Chain B 1–506（506 aa） Chain C 1–506（506 aa） Chain D 1–506（506 aa）	Not recorded	CYN CYANIDE ION × 2 HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.80 Å R-free 0.261
3J7B Catalase solved at 3.2 Angstrom resolution by MicroED Deposited 2014-06-09	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–527（527 aa） Chain B 1–527（527 aa） Chain C 1–527（527 aa） Chain D 1–527（527 aa）	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4	ELECTRON CRYSTALLOGRAPHY cryo-EM buffer pH 6.3 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.20 Å R-free 0.308
3NWL The crystal structure of the P212121 form of bovine liver catalase previously characterized by electron microscopy Deposited 2010-07-09	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–527（527 aa） Chain B 1–527（527 aa） Chain C 1–527（527 aa） Chain D 1–527（527 aa）	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4	X-RAY DIFFRACTION X-ray crystallization conditions sitting drop vapor diffusion using polymer-induced heteronucleation；pH 6.8；273 K；0.05 M sodium phosphate pH 6.8, 12% PEG 4000, sitting drop vapor diffusion using polymer-induced heteronucleation, temperature 273K	Resolution 2.69 Å R-free 0.241
3RE8 Structural and Kinetic Analysis of the Beef liver Catalase interacting with Nitric Oxide Deposited 2011-04-03	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 4–502（499 aa） Fragment：unp residues 4-502 Chain B 4–502（499 aa） Fragment：unp residues 4-502 Chain C 4–502（499 aa） Fragment：unp residues 4-502 Chain D 4–502（499 aa） Fragment：unp residues 4-502	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.4；277 K；45-60 mM Mg formate,12-13mg/ml protein containing 1-5 wt% of NH4OH (30% in water) soaking these crystals overnight in an 80 mM Mg-Formate solution, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 277 K	Resolution 1.90 Å R-free 0.259
3RGP Structural and Kinetic Analysis of the Beef liver Catalase complexed with Nitric Oxide Deposited 2011-04-08	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 4–502（499 aa） Fragment：unp residues 4-502 Chain B 4–502（499 aa） Fragment：unp residues 4-502 Chain C 4–502（499 aa） Fragment：unp residues 4-502 Chain D 4–502（499 aa） Fragment：unp residues 4-502	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4 NO NITRIC OXIDE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.7；298 K；1. 45-60mM Mg Formate mixed with 12-13 mg/ml protein containing 1-5 wt% of NH4OH. 2. Crystals then soaked overnight in 80 mM Mg-Formate solution, pH 6.7, 3. Finally soaked in 80 mM Mg formate and 150 mM bis-tris & 10-100mM DEANO, pH 6.5 , VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.88 Å R-free 0.214
3RGS Structural and kinetic analysis of the beef liver catalase with the ammonia as a ligand Deposited 2011-04-08	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 4–502（499 aa） Fragment：unp residues 4-502 Chain B 4–502（499 aa） Fragment：unp residues 4-502 Chain C 4–502（499 aa） Fragment：unp residues 4-502 Chain D 4–502（499 aa） Fragment：unp residues 4-502	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4 NH3 AMMONIA × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.7；298 K；45-60mM Mg Formate mixed with 12-13 mg/ml protein containing 1-5 wt% of NH4OH, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.99 Å R-free 0.198
4BLC THE STRUCTURE OF ORTHORHOMBIC CRYSTALS OF BEEF LIVER CATALASE Deposited 1998-09-27	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–506（506 aa） Chain B 1–506（506 aa） Chain C 1–506（506 aa） Chain D 1–506（506 aa）	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6.5；VAPOR DIFFUSION AGAINST 10% N-PROPANOL, AND 0.1 M NA-PO4 BUFFER PH 6.2 TO 6.8 DROP SET UP 15 UL OF 40 MG/ML PROTEIN PLUS 5 UL 1% NACL PLUS 5 UL RESERVOIR., pH 6.5, vapor diffusion	Resolution 2.30 Å R-free 0.273
5GKN Catalase structure determined by electron crystallography of thin 3D crystals Deposited 2016-07-04	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–527（527 aa） Chain B 1–527（527 aa） Chain C 1–527（527 aa） Chain D 1–527（527 aa）	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4	ELECTRON CRYSTALLOGRAPHY cryo-EM buffer pH 5.3 cryo-EM vitrification conditions Cryogen ETHANE X-ray crystallization conditions pH 5.3	Resolution 3.20 Å R-free 0.304
6JNT Catalase structure determined by eEFD (dataset 1) Deposited 2019-03-18	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–527（527 aa） Chain B 1–527（527 aa） Chain C 1–527（527 aa） Chain D 1–527（527 aa）	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4	ELECTRON CRYSTALLOGRAPHY cryo-EM buffer pH 5.3 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 3.00 Å R-free 0.283
6JNU Catalase structure determined by eEFD (dataset 2) Deposited 2019-03-18	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–527（527 aa） Chain B 1–527（527 aa） Chain C 1–527（527 aa） Chain D 1–527（527 aa）	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4	ELECTRON CRYSTALLOGRAPHY cryo-EM buffer pH 5.3 cryo-EM vitrification conditions Cryogen NITROGEN	Resolution 3.00 Å R-free 0.251
6PM7 The structure of the triclinic crystal form of beef liver catalase at 1.85 A resolution Deposited 2019-07-01	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 1–527（527 aa） Chain B 1–527（527 aa）	Mutation：N213D, N226D Mutation：N213D, N226D	HEM PROTOPORPHYRIN IX CONTAINING FE × 4 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；298 K；Vapor diffusion with 10 ul drops and 0.6 ml reservoirs. Reservoirs were 6% PEG 3350 buffered with 0.1 M MES at pH 6.5. Drops were equal amounts of 35 mg/ml protein in H2O and reservoir solution. Growth time about two weeks.	Resolution 1.85 Å R-free 0.232
6PO0 The structure of the orthorhombic (P212121) crystal form of beef liver catalase at 1.85 A resolution Deposited 2019-07-03	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 1–527（527 aa） Chain B 1–527（527 aa） Chain C 1–527（527 aa） Chain D 1–527（527 aa）	Mutation：N213D, N226D Mutation：N213D, N226D Mutation：N213D, N226D Mutation：N213D, N226D	HEM PROTOPORPHYRIN IX CONTAINING FE × 4 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；298 K；Crystals grown from 20 mM magnesium formate in 0.1 M Mes pH 6.5 reservoirs with drops equal amounts of 40 mg/ml catalase in water and the reservoir solution. Generally 2 to 6 days at room temperature.	Resolution 1.75 Å R-free 0.207
7CAT The NADPH binding site on beef liver catalase Deposited 1984-11-15	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: 4-MERIC	Chain A 1–506（506 aa） Chain B 1–506（506 aa）	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å
7DI8 Electron crystallographic structure of Catalase using a direct electron detector at 300 kV Deposited 2020-11-18	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–527（527 aa） Chain B 1–527（527 aa） Chain C 1–527（527 aa） Chain D 1–527（527 aa）	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4	ELECTRON CRYSTALLOGRAPHY cryo-EM buffer pH 5.3 X-ray crystallization conditions BATCH MODE；pH 5.3	Resolution 3.20 Å R-free 0.348
8CAT The NADPH binding site on beef liver catalase Deposited 1984-11-15	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 1–506（506 aa） Chain B 1–506（506 aa）	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å
9BDJ MicroED structure of bovine liver catalase with missing cone eliminated by suspended drop Deposited 2024-04-11	Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–527（527 aa） Chain B 1–527（527 aa） Chain C 1–527（527 aa） Chain D 1–527（527 aa）	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4	ELECTRON CRYSTALLOGRAPHY cryo-EM buffer pH 6.3 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 4.00 Å R-free 0.358

18 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CATA_BOVIN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–506； UniProt 1–506 Author chain B； PDBConstruct 1–506； UniProt 1–506 Author chain C； PDBConstruct 1–506； UniProt 1–506 Author chain D； PDBConstruct 1–506； UniProt 1–506

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	1th4
Deposition date deposition_date	2004-06-01
Structure title title	crystal structure of NADPH depleted bovine liver catalase complexed with 3-amino-1,2,4-triazole
Keywords keywords	bovine liver catalase, NADPH, 3-amino-1, 2, 4-triazole, 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	36.41 Å
Radius of gyration Rg (electron density) rg_electron	35.73 Å
Forward intensity I(0) i0	808405000.00
Molecular weight molecular_weight	229670.0 kDa
Excluded volume excluded_volume	285450 Å³
Envelope volume envelope_volume	333570 Å³
Hydration-shell volume shell_volume	72084 Å³
Envelope diameter envelope_diameter	116.3 Å
Shell Rg shell_rg	45.99 Å
Envelope Rg envelope_rg	35.80 Å
Shape Rg shape_rg	35.73 Å
Total Rg total_rg	36.29 Å
Total atoms total_atoms	16246
Residues n_residues	1996
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	110.1 Å
Rg (real space) rg_real	36.16 Å
Rg uncertainty (real space) rg_real_error	0.65 Å
I(0) (real space) i0_real	8.0840e+08
I(0) uncertainty (real space) i0_real_error	1.3140e+07
Rg (reciprocal space) rg_reciprocal	36.32 Å
I(0) (reciprocal space) i0_reciprocal	808500000.0000
Solution quality estimate total_estimate	0.8981
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	46.1 Å
Skewness Skewness skewness	0.132
Kurtosis Kurtosis kurtosis	-0.510
Angular range angular_range	— – 0.2150 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	294800000.0000
Real-space data points n_real_points	44
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.935; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.895

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	Catalase
Molecular weight formula_weight	57664.5 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	16915

ADNRDPASDQMKHWKEQRAAQKPDVLTTGGGNPVGDKLNSLTVGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITRYSKAKVFEHIGKRTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDALLFPSFIHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMDGYGSHTFKLVNADGEAVYCKFHYKTDQGIKNLSVEDAARLAHEDPDYGLRDLFNAIATGNYPSWTLYIQVMTFSEAEIFPFNPFDLTKVWPHGDYPLIPVGKLVLNRNPVNYFAEVEQLAFDPSNMPPGIEPSPDKMLQGRLFAYPDTHRHRLGPNYLQIPVNCPYRARVANYQRDGPMCMMDNQGGAPNYYPNSFSAPEHQPSALEHRTHFSGDVQRFNSANDDNVTQVRTFYLKVLNEEQRKRLCENIAGHLKDAQLFIQKKAVKNFSDVHPEYGSRIQALLDKYNEEKPKN

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 non-polymer

Description description	3-AMINO-1,2,4-TRIAZOLE
Molecular weight formula_weight	84.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	669

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7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1th4a_
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.5 — Heme-dependent catalase-like
Superfamily Superfamily superfamily	e.5.1 — Heme-dependent catalase-like
Family Family family	e.5.1.1 — Heme-dependent catalases

Domain ID domain_id	d1th4b_
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.5 — Heme-dependent catalase-like
Superfamily Superfamily superfamily	e.5.1 — Heme-dependent catalase-like
Family Family family	e.5.1.1 — Heme-dependent catalases

Domain ID domain_id	d1th4c_
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.5 — Heme-dependent catalase-like
Superfamily Superfamily superfamily	e.5.1 — Heme-dependent catalase-like
Family Family family	e.5.1.1 — Heme-dependent catalases

Domain ID domain_id	d1th4d_
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.5 — Heme-dependent catalase-like
Superfamily Superfamily superfamily	e.5.1 — Heme-dependent catalase-like
Family Family family	e.5.1.1 — Heme-dependent catalases

CATH v4.4 (12 domains)

Domain ID domain_id	1th4A01
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	91 — Cytochrome C Oxidase; Chain J
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1th4A02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	180 — Catalase HpII, Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Catalase core domain

Domain ID domain_id	1th4A03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1370 — Hemocyanin, N-terminal domain
Homologous superfamily homologous superfamily	60 —

Domain ID domain_id	1th4B01
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	91 — Cytochrome C Oxidase; Chain J
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1th4B02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	180 — Catalase HpII, Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Catalase core domain

Domain ID domain_id	1th4B03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1370 — Hemocyanin, N-terminal domain
Homologous superfamily homologous superfamily	60 —

Domain ID domain_id	1th4C01
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	91 — Cytochrome C Oxidase; Chain J
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1th4C02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	180 — Catalase HpII, Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Catalase core domain

Domain ID domain_id	1th4C03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1370 — Hemocyanin, N-terminal domain
Homologous superfamily homologous superfamily	60 —

Domain ID domain_id	1th4D01
Class class	4 — Few Secondary Structures
Architecture architecture	10 — Irregular
Topology topology	91 — Cytochrome C Oxidase; Chain J
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1th4D02
Class class	2 — Mainly Beta
Architecture architecture	40 — Beta Barrel
Topology topology	180 — Catalase HpII, Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Catalase core domain

Domain ID domain_id	1th4D03
Class class	1 — Mainly Alpha
Architecture architecture	20 — Up-down Bundle
Topology topology	1370 — Hemocyanin, N-terminal domain
Homologous superfamily homologous superfamily	60 —

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8. Citations (1)

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Unit-cell length a length_a	85.030 Å
Unit-cell length b length_b	141.090 Å
Unit-cell length c length_c	231.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	16

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.980 Å
Low-resolution limit resolution_low	39.900 Å
R factor r_factor	0.2350
R_work r_work	0.2350
R_free r_free	0.2920

fit	/app/data/saxs_computation/th/1th4/1th4.fit
pddf	/app/data/pr_computation/th/1th4/1th4.pr.out
profile	/app/data/saxs_computation/th/1th4/1th4.dat