SAXSdb — 1h3a

▼

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

SQUALENE--HOPENE CYCLASE

ALICYCLOBACILLUS ACIDOCALDARIUS

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE × 2 (2E)-N-ALLYL-4-{[3-(4-BROMOPHENYL)-5-FLUORO-1-METHYL-1H-INDAZOL-6-YL]OXY}-N-METHYL-2-BUTEN-1-AMINE × 2 water × 2	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 2	(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE × 2 (2E)-N-ALLYL-4-{[3-(4-BROMOPHENYL)-5-FLUORO-1-METHYL-1H-INDAZOL-6-YL]OXY}-N-METHYL-2-BUTEN-1-AMINE × 2 water × 2	Consistent with protein count
3	Protein homooligomer	Homooligomer	Protein 2	(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE × 2 (2E)-N-ALLYL-4-{[3-(4-BROMOPHENYL)-5-FLUORO-1-METHYL-1H-INDAZOL-6-YL]OXY}-N-METHYL-2-BUTEN-1-AMINE × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	SQHC_ALIAC
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–631； UniProt 1–630 Author chain B； PDBConstruct 2–631； UniProt 1–630 Author chain C； PDBConstruct 2–631； UniProt 1–630

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	1h3a
Deposition date deposition_date	2002-08-24
Structure title title	Structures of Human Oxidosqualene Cyclase Inhibitors Bound to an Homologous Enzyme
Keywords keywords	ISOMERASE, CHOLESTEROL BIOSYNTHESIS, INHIBITOR, MONOTOPIC MEMBRANE PROTEIN; ISOMERASE
Experimental Method method	X-RAY DIFFRACTION

▼

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.

1h3a__assembly_2__model_1

Assembly 2 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1h3a__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1h3a__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	36.33 Å
Rg (electron density)	35.42 Å
Total Rg	35.85 Å
Atom count	10026
Residues	1240
Excluded volume	177790 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1h3a__assembly_1__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`1h3a__assembly_2__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download
3	1	`1h3a__assembly_3__model_1`	dimeric （2）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	SQUALENE--HOPENE CYCLASE
Molecular weight formula_weight	71650.0 kDa
EC 编号 ec_number	5.4.99.17
Source method src_method	man
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	15281

MAEQLVEAPAYARTLDRAVEYLLSCQKDEGYWWGPLLSNVTMEAEYVLLCHILDRVDRDRMEKIRRYLLHEQREDGTWALYPGGPPDLDTTIEAYVALKYIGMSRDEEPMQKALRFIQSQGGIESSRVFTRMWLALVGEYPWEKVPMVPPEIMFLGKRMPLNIYEFGSWARATVVALSIVMSRQPVFPLPERARVPELYETDVPPRRRGAKGGGGWIFDALDRALHGYQKLSVHPFRRAAEIRALDWLLERQAGDGSWGGIQPPWFYALIALKILDMTQHPAFIKGWEGLELYGVELDYGGWMFQASISPVWDTGLAVLALRAAGLPADHDRLVKAGEWLLDRQITVPGDWAVKRPNLKPGGFAFQFDNVYYPDVDDTAVVVWALNTLRLPDERRRRDAMTKGFRWIVGMQSSNGGWGAYDVDNTSDLPNHIPFCDFGEVTDPPSEDVTAHVLECFGSFGYDDAWKVIRRAVEYLKREQKPDGSWFGRWGVNYLYGTGAVVSALKAVGIDTREPYIQKALDWVEQHQNPDGGWGEDCRSYEDPAYAGKGASTPSQTAWALMALIAGGRAESEAARRGVQYLVETQRPDGGWDEPYYTGTGFPGDFYLGYTMYRHVFPTLALGRYKQAIERR

Source Source

Source organism organism	ALICYCLOBACILLUS ACIDOCALDARIUS
NCBI taxonomy ID ncbi_taxonomy_id	405212
Host organism host_organism	ESCHERICHIA COLI K-12

Entity 2 Entity 2 non-polymer

Description description	(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE
Molecular weight formula_weight	306.4 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 3 Entity 3 non-polymer

Description description	(2E)-N-ALLYL-4-{[3-(4-BROMOPHENYL)-5-FLUORO-1-METHYL-1H-INDAZOL-6-YL]OXY}-N-METHYL-2-BUTEN-1-AMINE
Molecular weight formula_weight	444.3 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	242

▼

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

Domain ID domain_id	d1h3aa1
Class class	a — All alpha proteins
Fold Fold fold	a.102 — alpha/alpha toroid
Superfamily Superfamily superfamily	a.102.4 — Terpenoid cyclases/Protein prenyltransferases
Family Family family	a.102.4.2 — Terpene synthases

Domain ID domain_id	d1h3aa2
Class class	a — All alpha proteins
Fold Fold fold	a.102 — alpha/alpha toroid
Superfamily Superfamily superfamily	a.102.4 — Terpenoid cyclases/Protein prenyltransferases
Family Family family	a.102.4.2 — Terpene synthases

Domain ID domain_id	d1h3ab1
Class class	a — All alpha proteins
Fold Fold fold	a.102 — alpha/alpha toroid
Superfamily Superfamily superfamily	a.102.4 — Terpenoid cyclases/Protein prenyltransferases
Family Family family	a.102.4.2 — Terpene synthases

Domain ID domain_id	d1h3ab2
Class class	a — All alpha proteins
Fold Fold fold	a.102 — alpha/alpha toroid
Superfamily Superfamily superfamily	a.102.4 — Terpenoid cyclases/Protein prenyltransferases
Family Family family	a.102.4.2 — Terpene synthases

Domain ID domain_id	d1h3ac1
Class class	a — All alpha proteins
Fold Fold fold	a.102 — alpha/alpha toroid
Superfamily Superfamily superfamily	a.102.4 — Terpenoid cyclases/Protein prenyltransferases
Family Family family	a.102.4.2 — Terpene synthases

Domain ID domain_id	d1h3ac2
Class class	a — All alpha proteins
Fold Fold fold	a.102 — alpha/alpha toroid
Superfamily Superfamily superfamily	a.102.4 — Terpenoid cyclases/Protein prenyltransferases
Family Family family	a.102.4.2 — Terpene synthases

CATH v4.4 (6 domains)

Domain ID domain_id	1h3aA01
Class class	1 — Mainly Alpha
Architecture architecture	50 — Alpha/alpha barrel
Topology topology	10 — Glycosyltransferase
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1h3aA02
Class class	1 — Mainly Alpha
Architecture architecture	50 — Alpha/alpha barrel
Topology topology	10 — Glycosyltransferase
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1h3aB01
Class class	1 — Mainly Alpha
Architecture architecture	50 — Alpha/alpha barrel
Topology topology	10 — Glycosyltransferase
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1h3aB02
Class class	1 — Mainly Alpha
Architecture architecture	50 — Alpha/alpha barrel
Topology topology	10 — Glycosyltransferase
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1h3aC01
Class class	1 — Mainly Alpha
Architecture architecture	50 — Alpha/alpha barrel
Topology topology	10 — Glycosyltransferase
Homologous superfamily homologous superfamily	20 —

Domain ID domain_id	1h3aC02
Class class	1 — Mainly Alpha
Architecture architecture	50 — Alpha/alpha barrel
Topology topology	10 — Glycosyltransferase
Homologous superfamily homologous superfamily	20 —

▶

Unit-cell length a length_a	140.904 Å
Unit-cell length b length_b	140.904 Å
Unit-cell length c length_c	243.832 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	120.00 °
Molecules per unit cell Z z_pdb	18

Space group space_group	P 32 2 1
Space-group number int_tables_number	154
Crystal system crystal_system	—

Resolution resolution	2.850 Å
Low-resolution limit resolution_low	25.000 Å
R factor r_factor	0.2480
R_work r_work	0.2480
R_free r_free	0.2700

Structures of Human Oxidosqualene Cyclase Inhibitors Bound to an Homologous Enzyme

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

SQUALENE--HOPENE CYCLASE

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

1h3a__assembly_2__model_1

1h3a__assembly_2__model_1 | I(q)

1h3a__assembly_2__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

CATH v4.4 (6 domains)

7. Citations (5)

Structures of Human Oxidosqualene Cyclase Inhibitors Bound to an Homologous Enzyme

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

SQUALENE--HOPENE CYCLASE

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

1h3a__assembly_2__model_1

1h3a__assembly_2__model_1 | I(q)

1h3a__assembly_2__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 (4)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 water

6. Fold Classification (SCOP + CATH) 12 domains

SCOP 2.08 (6 domains)

CATH v4.4 (6 domains)

7. Citations (5)