SAXSdb — 2q01

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

Uronate isomerase

Caulobacter crescentus

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 3	POTASSIUM ION × 3 water × 3	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	UXAC_CAUCR
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 4–489； UniProt 1–486 Author chain B； PDBConstruct 4–489； UniProt 1–486 Author chain C； PDBConstruct 4–489； UniProt 1–486

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	2q01
Deposition date deposition_date	2007-05-18
Structure title title	Crystal structure of glucuronate isomerase from Caulobacter crescentus
Keywords keywords	ISOMERASE, STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, PSI, New York SGX Research Center for Structural Genomics, NYSGXRC; ISOMERASE
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.

2q01__assembly_1__model_1

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

Download this curve (.dat)

2q01__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2q01__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	33.61 Å
Rg (electron density)	32.56 Å
Total Rg	33.17 Å
Atom count	11533
Residues	1439
Excluded volume	202940 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2q01__assembly_1__model_1`	trimeric （3）	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	Uronate isomerase
Molecular weight formula_weight	56339.9 kDa
EC 编号 ec_number	5.3.1.12
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	12130

MSLARPLSFHEDRLFPSDPATRSYARGLYALVKDLPIISPHGHTDPSWFATNAPFQDATDLLLAPDHYLFRMLYSQGVSLDALKVRSKAGVPDTDPREAWRVFASHFYLFRGTPSWVWLNHVFSQVFGFTEFLEASNADDYFDRITAALATDAFRPRALFDRFNIETLATTEGPHESLQHHAAIRESGWGGHVITAYRPDAVIDFEDERSPRAFERFAETSGQDVYSWKSYLEAHRLRRQAFIDAGATSSDHGHPTAATADLSDVEAEALFNSLVKGDVTPEKAELFRAQMLTEMAKMSLDDGLVMQIHPGSHRNHNVGLLNSHGRDKGADIPMRTEYVDALKPLLTRLGNDPRLSIILFTLDETTYSRELAPLAGHYPVLKLGPSWWFHDSPEGMMRFREQVTETAGFYNTVGFNDDTRAFLSIPARHDVARRVDSAFLARMVAEHRMDLVEAEELIVDLTYNLPKKAYKLDQRPDWARPATLRAAAEEGHHHHHH

Source Source

Source organism organism	Caulobacter crescentus
NCBI taxonomy ID ncbi_taxonomy_id	190650
Host organism host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 non-polymer

Description description	POTASSIUM ION
Molecular weight formula_weight	39.1 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	488

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6. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d2q01a_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.9 — Metallo-dependent hydrolases
Family Family family	c.1.9.0 — automated matches

Domain ID domain_id	d2q01b_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.9 — Metallo-dependent hydrolases
Family Family family	c.1.9.0 — automated matches

Domain ID domain_id	d2q01c_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamily	c.1.9 — Metallo-dependent hydrolases
Family Family family	c.1.9.0 — automated matches

CATH v4.4 (6 domains)

Domain ID domain_id	2q01A01
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	140 — Metal-dependent hydrolases

Domain ID domain_id	2q01A02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	2020 — uronate isomerase, domain 2, chain A
Homologous superfamily homologous superfamily	10 — uronate isomerase, domain 2, chain A

Domain ID domain_id	2q01B01
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	140 — Metal-dependent hydrolases

Domain ID domain_id	2q01B02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	2020 — uronate isomerase, domain 2, chain A
Homologous superfamily homologous superfamily	10 — uronate isomerase, domain 2, chain A

Domain ID domain_id	2q01C01
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	20 — TIM Barrel
Homologous superfamily homologous superfamily	140 — Metal-dependent hydrolases

Domain ID domain_id	2q01C02
Class class	1 — Mainly Alpha
Architecture architecture	10 — Orthogonal Bundle
Topology topology	2020 — uronate isomerase, domain 2, chain A
Homologous superfamily homologous superfamily	10 — uronate isomerase, domain 2, chain A

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Unit-cell length a length_a	177.332 Å
Unit-cell length b length_b	190.176 Å
Unit-cell length c length_c	319.290 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	48

Space group space_group	F 2 2 2
Space-group number int_tables_number	22
Crystal system crystal_system	—

Resolution resolution	2.340 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.1997
R_work r_work	0.1982
R_free r_free	0.2512

Crystal structure of glucuronate isomerase from Caulobacter crescentus

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

Uronate isomerase

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

2q01__assembly_1__model_1

2q01__assembly_1__model_1 | I(q)

2q01__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) 9 domains

SCOP 2.08 (3 domains)

CATH v4.4 (6 domains)

7. Citations (1)

Crystal structure of glucuronate isomerase from Caulobacter crescentus

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

Uronate isomerase

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

2q01__assembly_1__model_1

2q01__assembly_1__model_1 | I(q)

2q01__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) 9 domains

SCOP 2.08 (3 domains)

CATH v4.4 (6 domains)

7. Citations (1)