SAXSdb — 3g0i

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

Epoxide hydrolase

Aspergillus niger

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	2-PROPYLPENTANAMIDE × 2 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q9UR30_ASPNG
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 3–394； UniProt 5–396 Author chain B； PDBConstruct 3–394； UniProt 5–396

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	3g0i
Deposition date deposition_date	2009-01-28
Structure title title	Complex of Aspergillus niger epoxide hydrolase with valpromide (2-propylpentanamide)
Keywords keywords	Epoxide hydrolase, alpha/beta hydrolase fold, valpromide, 2-propylpentanamide, Hydrolase; 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.

3g0i__assembly_1__model_1

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

Download this curve (.dat)

3g0i__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3g0i__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	29.87 Å
Rg (electron density)	29.13 Å
Total Rg	29.75 Å
Atom count	6148
Residues	770
Excluded volume	110210 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3g0i__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 (3)

Entity 1 Entity 1 polymer

Description description	Epoxide hydrolase
Molecular weight formula_weight	44124.2 kDa
EC 编号 ec_number	3.3.2.9
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	6692

KAFAKFPSSASISPNPFTVSIPDEQLDDLKTLVRLSKIAPPTYESLQADGRFGITSEWLTTMREKWLSEFDWRPFEARLNSFPQFTTEIEGLTIHFAALFSEREDAVPIALLHGWPGSFVEFYPILQLFREEYTPETLPFHLVVPSLPGYTFSSGPPLDKDFGLMDNARVVDQLMKDLGFGSGYIIQGGDIGSFVGRLLGVGFDACKAVHLNLCAMRAPPEGPSIESLSAAEKEGIARMEKFMTDGLAYAMEHSTRPSTIGHVLSSSPIALLAWIGEKYLQWVDKPLPSETILEMVSLYWLTESFPRAIHTYRETTPTASAPNGATMLQKELYIHKPFGFSFFPKDLCPVPRSWIATTGNLVFFRDHAEGGHFAALERPRELKTDLTAFVEQVW

Source Source

Source organism organism	Aspergillus niger
NCBI taxonomy ID ncbi_taxonomy_id	5061
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	2-PROPYLPENTANAMIDE
Molecular weight formula_weight	143.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	454

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6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d3g0ia1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.69 — alpha/beta-Hydrolases
Superfamily Superfamily superfamily	c.69.1 — alpha/beta-Hydrolases
Family Family family	c.69.1.11 — Epoxide hydrolase

Domain ID domain_id	d3g0ia2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d3g0ib1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.69 — alpha/beta-Hydrolases
Superfamily Superfamily superfamily	c.69.1 — alpha/beta-Hydrolases
Family Family family	c.69.1.11 — Epoxide hydrolase

Domain ID domain_id	d3g0ib2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id	3g0iA00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1820 — Alpha/Beta hydrolase fold, catalytic domain

Domain ID domain_id	3g0iB00
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	50 — Rossmann fold
Homologous superfamily homologous superfamily	1820 — Alpha/Beta hydrolase fold, catalytic domain

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Unit-cell length a length_a	62.985 Å
Unit-cell length b length_b	89.655 Å
Unit-cell length c length_c	75.812 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	105.31 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.100 Å
Low-resolution limit resolution_low	38.210 Å
R factor r_factor	0.1760
R_work r_work	0.1750
R_free r_free	0.2220

Complex of Aspergillus niger epoxide hydrolase with valpromide (2-propylpentanamide)

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

Epoxide hydrolase

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

3g0i__assembly_1__model_1

3g0i__assembly_1__model_1 | I(q)

3g0i__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

CATH v4.4 (2 domains)

7. Citations (2)

Complex of Aspergillus niger epoxide hydrolase with valpromide (2-propylpentanamide)

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

Epoxide hydrolase

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

3g0i__assembly_1__model_1

3g0i__assembly_1__model_1 | I(q)

3g0i__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 (3)

Entity 1 Entity 1 polymer

Polymer Polymer

Source Source

Entity 2 Entity 2 non-polymer

Entity 3 Entity 3 water

6. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

CATH v4.4 (2 domains)

7. Citations (2)