SAXSdb — 1h41

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

ALPHA-GLUCURONIDASE

PSEUDOMONAS CELLULOSA

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 2	4-O-methyl-alpha-D-glucopyranuronic acid × 2 1,2-ETHANEDIOL × 28 COBALT (II) ION × 10 water × 2	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	Q8VP74
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–708； UniProt 25–732 Author chain B； PDBConstruct 1–708； UniProt 25–732

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	1h41
Deposition date deposition_date	2002-09-25
Structure title title	Pseudomonas cellulosa E292A alpha-D-glucuronidase mutant complexed with aldotriuronic acid
Keywords keywords	HYDROLASE, GLUCURONIDASE, (ALPHA-BETA)8 BARREL, GLYCOSIDE HYDROLASE, GLUCURONIC ACID; 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.

1h41__assembly_1__model_1

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

Download this curve (.dat)

1h41__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

1h41__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	34.66 Å
Rg (electron density)	33.80 Å
Total Rg	34.48 Å
Atom count	11383
Residues	1401
Excluded volume	201300 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`1h41__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 (5)

Entity 1 Entity 1 polymer

Description description	ALPHA-GLUCURONIDASE
Molecular weight formula_weight	80381.6 kDa
EC 编号 ec_number	3.2.1.139
Mutation mutation	YES
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	13218

EDGYDMWLRYQPIADQTLLKTYQKQIRHLHVAGDSPTINAAAAELQRGLSGLLNKPIVARDEKLKDYSLVIGTPDNSPLIASLNLGERLQALGAEGYLLEQTRINKRHVVIVAANSDVGVLYGSFHLLRLIQTQHALEKLSLSSAPRLQHRVVNHWDNLNRVVERGYAGLSLWDWGSLPNYLAPRYTDYARINASLGINGTVINNVNADPRVLSDQFLQKIAALADAFRPYGIKMYLSINFNSPRAFGDVDTADPLDPRVQQWWKTRAQKIYSYIPDFGGFLVKADSAGQPGPQGYGRDHAEGANMLAAALKPFGGVVFWRAFVYHPDIEDRFRGAYDEFMPLDGKFADNVILQIKNGPIDFQPREPFSALFAGMSRTNMMMEFQITQEYFGFATHLAYQGPLFEESLKTETHARGEGSTIGNILEGKVFKTRHTGMAGVINPGTDRNWTGHPFVQSSWYAFGRMAWDHQISAATAADEWLRMTFSNQPAFIEPVKQMMLVSREAGVNYRSPLGLTHLYSQGDHYGPAPWTDDLPRADWTAVYYHRASKTGIGFNRTKTGSNALAQYPEPIAKAWGDLNSVPEDLILWFHHLSWDHRMQSGRNLWQELVHKYYQGVEQVRAMQRTWDQQEAYVDAARFAQVKALLQVQEREAVRWRNSCVLYFQSVAGRPIPANYEQPEHDLEYYKMLARTTYVPEPWHPASSSRVLK

Source Source

Source organism organism	PSEUDOMONAS CELLULOSA
NCBI taxonomy ID ncbi_taxonomy_id	155077
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 non-polymer

Description description	4-O-methyl-alpha-D-glucopyranuronic acid
Molecular weight formula_weight	208.2 kDa
Source method src_method	man
Copy count entity_count	2

Entity 3 Entity 3 non-polymer

Description description	1,2-ETHANEDIOL
Molecular weight formula_weight	62.1 kDa
Source method src_method	syn
Copy count entity_count	28

Entity 4 Entity 4 non-polymer

Description description	COBALT (II) ION
Molecular weight formula_weight	58.9 kDa
Source method src_method	syn
Copy count entity_count	10

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1667

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6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

Domain ID domain_id	d1h41a1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.8 — (Trans)glycosidases
Family Family family	c.1.8.10 — alpha-D-glucuronidase/Hyaluronidase catalytic domain

Domain ID domain_id	d1h41a2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.92 — Zincin-like
Superfamily Superfamily superfamily	d.92.2 — beta-N-acetylhexosaminidase-like domain
Family Family family	d.92.2.2 — alpha-D-glucuronidase, N-terminal domain

Domain ID domain_id	d1h41b1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.8 — (Trans)glycosidases
Family Family family	c.1.8.10 — alpha-D-glucuronidase/Hyaluronidase catalytic domain

Domain ID domain_id	d1h41b2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.92 — Zincin-like
Superfamily Superfamily superfamily	d.92.2 — beta-N-acetylhexosaminidase-like domain
Family Family family	d.92.2.2 — alpha-D-glucuronidase, N-terminal domain

CATH v4.4 (6 domains)

Domain ID domain_id	1h41A01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	379 — Chitobiase; domain 2
Homologous superfamily homologous superfamily	10 — Chitobiase/beta-hexosaminidase domain 2-like

Domain ID domain_id	1h41A02
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	80 — Glycosidases

Domain ID domain_id	1h41A03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1330 — Alpha-d-glucuronidase, C-terminal Domain
Homologous superfamily homologous superfamily	10 — Alpha-glucuronidase, C-terminal domain

Domain ID domain_id	1h41B01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	379 — Chitobiase; domain 2
Homologous superfamily homologous superfamily	10 — Chitobiase/beta-hexosaminidase domain 2-like

Domain ID domain_id	1h41B02
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	80 — Glycosidases

Domain ID domain_id	1h41B03
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1330 — Alpha-d-glucuronidase, C-terminal Domain
Homologous superfamily homologous superfamily	10 — Alpha-glucuronidase, C-terminal domain

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Unit-cell length a length_a	69.412 Å
Unit-cell length b length_b	74.393 Å
Unit-cell length c length_c	87.462 Å
Unit-cell angle α angle_alpha	115.09 °
Unit-cell angle β angle_beta	93.04 °
Unit-cell angle γ angle_gamma	109.44 °
Molecules per unit cell Z z_pdb	2

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

Resolution resolution	1.500 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.1180
R_work r_work	0.1180
R_free r_free	0.1530

Pseudomonas cellulosa E292A alpha-D-glucuronidase mutant complexed with aldotriuronic acid

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

ALPHA-GLUCURONIDASE

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

1h41__assembly_1__model_1

1h41__assembly_1__model_1 | I(q)

1h41__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 (5)

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 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

CATH v4.4 (6 domains)

7. Citations (1)

Pseudomonas cellulosa E292A alpha-D-glucuronidase mutant complexed with aldotriuronic acid

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

ALPHA-GLUCURONIDASE

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

1h41__assembly_1__model_1

1h41__assembly_1__model_1 | I(q)

1h41__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 (5)

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 non-polymer

Entity 5 Entity 5 water

6. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (4 domains)

CATH v4.4 (6 domains)

7. Citations (1)