SAXSdb — 3f75

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

Cathepsin L Protease

Toxoplasma gondii

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	CHLORIDE ION × 2 BROMIDE ION × 1 1,2-ETHANEDIOL × 1 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q6DMN0_TOXGO
Isoform	—
PDB entities	1, 2
Chains and sequence ranges	Author chain A； PDBConstruct 1–224； UniProt 199–422 Author chain P； PDBConstruct 13–106； UniProt 105–198

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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	3f75
Deposition date deposition_date	2008-11-07
Structure title title	Activated Toxoplasma gondii cathepsin L (TgCPL) in complex with its propeptide
Keywords keywords	MEDICAL STRUCTURAL GENOMICS OF PATHOGENIC PROTOZOA, MSGPP, cysteine protease, parasite, protozoa, Hydrolase, Thiol protease; HYDROLASE
Experimental Method method	X-RAY DIFFRACTION

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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

3f75__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

3f75__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3f75__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	20.33 Å
Rg (electron density)	19.56 Å
Total Rg	20.46 Å
Atom count	2351
Residues	298
Excluded volume	41345 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3f75__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	Cathepsin L Protease
Molecular weight formula_weight	24428.5 kDa
EC 编号 ec_number	3.4.22.15
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	2544

NVLPSELPAGVDWRSRGCVTPVKDQRDCGSCWAFSTTGALEGAHCAKTGKLVSLSEQELMDCSRAEGNQSCSGGEMNDAFQYVLDSGGICSEDAYPYLARDEECRAQSCEKVVKILGFKDVPRRSEAAMKAALAKSPVSIAIEADQMPFQFYHEGVFDASCGTDLDHGVLLVGYGTDKESKKDFWIMKNSWGTGWGRDGYMYMAMHKGEEGQCGLLLDASFPVM

Source Source

Source organism organism	Toxoplasma gondii
NCBI taxonomy ID ncbi_taxonomy_id	383379
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 polymer

Description description	Cathepsin L Propeptide
Molecular weight formula_weight	12794.4 kDa
EC 编号 ec_number	3.4.22.15
Mutation mutation	N-terminal His tag replaced all but the last 94 residues of the propeptide domain
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	P

MRGSHHHHHHGSIWEWKEAHFQDAFSSFQAMYAKSYATEEEKQRRYAIFKNNLVYIHTHNQQGYSYSLKMNHFGDLSRDEFRRKYLGFKKSRNLKSHHLGVATELL

Source Source

Source organism organism	Toxoplasma gondii
NCBI taxonomy ID ncbi_taxonomy_id	383379
Host organism host_organism	Escherichia coli

Entity 3 Entity 3 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	BROMIDE ION
Molecular weight formula_weight	79.9 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 5 Entity 5 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	165

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6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d3f75a_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.3 — Cysteine proteinases
Superfamily Superfamily superfamily	d.3.1 — Cysteine proteinases
Family Family family	d.3.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id	3f75A00
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	70 — Cathepsin B; Chain A
Homologous superfamily homologous superfamily	10 — Cysteine proteinases

Domain ID domain_id	3f75P00
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	287 — Helix Hairpins
Homologous superfamily homologous superfamily	2250 —

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Unit-cell length a length_a	65.621 Å
Unit-cell length b length_b	65.621 Å
Unit-cell length c length_c	149.772 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 43 21 2
Space-group number int_tables_number	96
Crystal system crystal_system	—

Resolution resolution	1.990 Å
Low-resolution limit resolution_low	33.980 Å
R factor r_factor	0.1674
R_work r_work	0.1654
R_free r_free	0.2056

Activated Toxoplasma gondii cathepsin L (TgCPL) in complex with its propeptide

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

Cathepsin L Protease

State in the Current Structure

Other States of the Same Protein in the Database

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

3f75__assembly_1__model_1

3f75__assembly_1__model_1 | I(q)

3f75__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

CATH v4.4 (2 domains)

7. Citations (1)

Activated Toxoplasma gondii cathepsin L (TgCPL) in complex with its propeptide

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

Cathepsin L Protease

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

2. Structure Basics 2. Structure Basics

3. Official assembly/model SAXS Official SAXS Profiles

3f75__assembly_1__model_1

3f75__assembly_1__model_1 | I(q)

3f75__assembly_1__model_1 | P(r) · Pending

4. Crystallography and Experiment 4. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

5. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 polymer

Polymer Polymer

Source Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

CATH v4.4 (2 domains)

7. Citations (1)