1dgh

HUMAN ERYTHROCYTE CATALASE 3-AMINO-1,2,4-TRIAZOLE COMPLEX

Method: X-RAY DIFFRACTION D_max: 110.5 Å Quality: GOOD

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

PROTEIN (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 3–500 Chain B； UniProt 3–500 Chain C； UniProt 3–500 Chain D； UniProt 3–500	Non-standard monomer：Yes (specific site not provided by mmCIF)	HEM PROTOPORPHYRIN IX CONTAINING FE × 4 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION；pH 8；298 K；6.5 - 8.0% PEG4000, PROTEIN AT 40 MG/ML IN 50MM TRISCL, PH 8.0, VAPOR DIFFUSION, temperature 298K	Resolution 2.00 Å R-free 0.210

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 1DGH	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1DGB HUMAN ERYTHROCYTE CATALASE Deposited 1999-11-23	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 4–501（498 aa） Chain B 4–501（498 aa） Chain C 4–501（498 aa） Chain D 4–501（498 aa）	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；6.5 - 8.0% PEG4000, protein at 40 mg/mL in 50 mM TrisCl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 2.20 Å R-free 0.227
1DGF HUMAN ERYTHROCYTE CATALASE Deposited 1999-11-24	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 5–501（497 aa） Chain B 5–501（497 aa） Chain C 5–501（497 aa） Chain D 5–501（497 aa）	Not recorded	ACT ACETATE ION × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；298 K；6.5 - 8.0% PEG4000, PROTEIN AT 40 MG/ML IN 50MM TRISCL, PH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 1.50 Å R-free 0.192
1DGG HUMAN ERYTHROCYTE CATALSE CYANIDE COMPLEX Deposited 1999-11-24	Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 5–501（497 aa） Chain B 5–501（497 aa） Chain C 5–501（497 aa） Chain D 5–501（497 aa）	Not recorded	CYN CYANIDE ION × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 8；298 K；6.5 - 8.0% PEG4000, PROTEIN AT 40 MG/ML IN 50MM TRISCL, PH 8.0, VAPOR DIFFUSION, temperature 298K	Resolution 1.80 Å R-free 0.221
1F4J STRUCTURE OF TETRAGONAL CRYSTALS OF HUMAN ERYTHROCYTE CATALASE Deposited 2000-06-07	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） Fragment：INTACT BUT LACKS THE FIRST AND LAST EXONS Chain B 1–527（527 aa） Fragment：INTACT BUT LACKS THE FIRST AND LAST EXONS Chain C 1–527（527 aa） Fragment：INTACT BUT LACKS THE FIRST AND LAST EXONS Chain D 1–527（527 aa） Fragment：INTACT BUT LACKS THE FIRST AND LAST EXONS	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；potassium sodium tartrate, HEPES, sodium acetate, potassium chloride, 2-mercaptoethanol, EDTA, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 2.40 Å R-free 0.244
1QQW CRYSTAL STRUCTURE OF HUMAN ERYTHROCYTE CATALASE Deposited 1999-06-09	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）	Not recorded	HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.7；298 K；PROTEIN SOLUTION: 8MG/ML PROTEIN, 50MM KCL, 1MM 2-MERCAPTOETHANOL, 0.2MM EDTA, 20MM NAOAC PH 5.2; RESERVOIR: 6-7% PEG-20000, 0.1 M MES PH 6.7; DROPS WERE SET UP BY MIXING EQUAL VOLUMES OF PROTEIN SOLUTION AND RESERVOIR., VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 2.75 Å R-free 0.272
7P8W Human erythrocyte catalase cryoEM Deposited 2021-07-23	Different construct Different mutation/modification 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	NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE；Controlled environment plunge-freezer (Bellare et al, 1988; Technion University)	Resolution 2.20 Å
7VD9 2.29 A structure of the human catalase Deposited 2021-09-06	Different construct Different mutation/modification 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 MICROSCOPY cryo-EM buffer pH 6.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.29 Å
8EL9 Cryo-EM structure of human catalase Deposited 2022-09-23	Different construct Different mutation/modification 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 MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.27 Å
8HID HUMAN ERYTHROCYTE CATALSE COMPLEXED WITH BT-Br Deposited 2022-11-19	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）	Not recorded	LLR (~{S})-azanyl-[2-[[3-bromanyl-4-(diethylamino)phenyl]methyl]hydrazinyl]methanethiol × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1M MES pH6.8, 7% PEG20000	Resolution 2.20 Å R-free 0.265
8PVD Structure of catalase determined by cryoEM at 100 keV Deposited 2023-07-17	Different construct Different mutation/modification 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）	Not recorded	NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 3.40 Å
8SGV human liver mitochondrial Catalase Deposited 2023-04-13	Different construct Different mutation/modification 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 MICROSCOPY cryo-EM buffer pH 7.5 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.58 Å
8WZH Human erythrocyte catalase with SLS as additive during cryo-EM grid preparation Deposited 2023-11-01	Different construct Different mutation/modification 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 MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；Blot force, 0	Resolution 3.70 Å
8WZJ Human erythrocyte catalase Deposited 2023-11-01	Different construct Different mutation/modification 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 MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.70 Å
8WZK Human erythrocyte catalase Deposited 2023-11-01	Different construct Different mutation/modification 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 MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 2.40 Å
8WZM Human erythrocyte catalase with CTAB as additive during EM sample preparation Deposited 2023-11-02	Different construct Different mutation/modification 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 MICROSCOPY cryo-EM buffer pH 8 cryo-EM vitrification conditions Cryogen ETHANE；Blot force, 0	Resolution 2.70 Å
9T0K Catalase CryoEM Structure from Human erythrocyte at 1.87A resolution Deposited 2025-10-17	Different construct Different mutation/modification 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）	Not recorded	NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4 HEM PROTOPORPHYRIN IX CONTAINING FE × 4	ELECTRON MICROSCOPY cryo-EM buffer pH 7.4 cryo-EM vitrification conditions Cryogen ETHANE	Resolution 1.87 Å

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	CATA_HUMAN
Isoform	—
PDB entities	1, 2
Chains and sequence ranges	Author chain A； PDBConstruct 1–498； UniProt 3–500 Author chain C； PDBConstruct 1–498； UniProt 3–500 Author chain B； PDBConstruct 1–498； UniProt 3–500 Author chain D； PDBConstruct 1–498； UniProt 3–500

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	1dgh
Deposition date deposition_date	1999-11-24
Structure title title	HUMAN ERYTHROCYTE CATALASE 3-AMINO-1,2,4-TRIAZOLE COMPLEX
Keywords keywords	CATALASE, HEME, NADPH, HYDROGEN PEROXIDE, 3-AMINO-1, 2, 4-TRIAZOLE, INHIBITOR, 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	36.53 Å
Radius of gyration Rg (electron density) rg_electron	35.81 Å
Forward intensity I(0) i0	816418000.00
Molecular weight molecular_weight	230580.0 kDa
Excluded volume excluded_volume	286470 Å³
Envelope volume envelope_volume	333500 Å³
Hydration-shell volume shell_volume	72038 Å³
Envelope diameter envelope_diameter	116.7 Å
Shell Rg shell_rg	45.95 Å
Envelope Rg envelope_rg	35.82 Å
Shape Rg shape_rg	35.80 Å
Total Rg total_rg	36.39 Å
Total atoms total_atoms	16306
Residues n_residues	1989
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	110.5 Å
Rg (real space) rg_real	36.29 Å
Rg uncertainty (real space) rg_real_error	0.61 Å
I(0) (real space) i0_real	8.1640e+08
I(0) uncertainty (real space) i0_real_error	1.1070e+07
Rg (reciprocal space) rg_reciprocal	36.44 Å
I(0) (reciprocal space) i0_reciprocal	816500000.0000
Solution quality estimate total_estimate	0.8977
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	46.2 Å
Skewness Skewness skewness	0.133
Kurtosis Kurtosis kurtosis	-0.515
Angular range angular_range	— – 0.2150 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	288200000.0000
Real-space data points n_real_points	44
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.937; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.882

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	PROTEIN (CATALASE)
Molecular weight formula_weight	56713.4 kDa
EC 编号 ec_number	1.11.1.6
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C
Atom count atom_count	17815

SRDPASDQMQHWKEQRAAQKADVLTTGAGNPVGDKLNVITVGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYSKAKVFEHIGKKTPIAVRFSTVAGESGSADTVRDPRGFAVKFYTEDGNWDLVGNNTPIFFIRDPILFPSFIHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVSFLFSDRGIPDGHRHMNGYGSHTFKLVNANGEAVYCKFHYKTDQGIKNLSVEDAARLSQEDPDYGIRDLFNAIATGKYPSWTFYIQVMTFNQAETFPFNPFDLTKVWPHKDYPLIPVGKLVLNRNPVNYFAEVEQIAFDPSNMPPGIEASPDKMLQGRLFAYPDTHRHRLGPNYLHIPVNCPYRARVANYQRDGPMCMQDNQGGAPNYYPNSFGAPEQQPSALEHSIQYSGEVRRFNTANDDNVTQVRAFYVNVLNEEQRKRLCENIAGHLKDAQIFIQKKAVKNFTEVHPDYGSHIQALLDKYN

Entity 2 Entity 2 polymer

Description description	PROTEIN (CATALASE)
Molecular weight formula_weight	56794.5 kDa
EC 编号 ec_number	1.11.1.6
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D

Entity 3 Entity 3 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 4 Entity 4 non-polymer

Description description	NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE
Molecular weight formula_weight	745.4 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1469

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7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1dgha_
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	d1dghb_
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	d1dghc_
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	d1dghd_
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	1dghA01
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	1dghA02
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	1dghA03
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	1dghB01
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	1dghB02
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	1dghB03
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	1dghC01
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	1dghC02
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	1dghC03
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	1dghD01
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	1dghD02
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	1dghD03
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	84.028 Å
Unit-cell length b length_b	140.639 Å
Unit-cell length c length_c	231.346 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	8

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

Resolution resolution	2.000 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.1770
R_work r_work	0.1730
R_free r_free	0.2100

fit	/app/data/saxs_computation/dg/1dgh/1dgh.fit
pddf	/app/data/pr_computation/dg/1dgh/1dgh.pr.out
profile	/app/data/saxs_computation/dg/1dgh/1dgh.dat

HUMAN ERYTHROCYTE CATALASE 3-AMINO-1,2,4-TRIAZOLE COMPLEX

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

PROTEIN (CATALASE)

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

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

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 polymer

Polymer Polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

7. Fold Classification (SCOP + CATH) 16 domains

SCOP 2.08 (4 domains)

CATH v4.4 (12 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)