2wcv

Crystal structure of bacterial FucU

Method: X-RAY DIFFRACTION

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

L-FUCOSE MUTAROTASE

ESCHERICHIA COLI

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein homooligomer	Homooligomer	Protein 10	alpha-L-fucopyranose × 10 water × 10	Consistent with protein count
2	Protein homooligomer	Homooligomer	Protein 10	alpha-L-fucopyranose × 10 water × 10	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	FUCM_ECOHS
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–140； UniProt 1–140 Author chain B； PDBConstruct 1–140； UniProt 1–140 Author chain C； PDBConstruct 1–140； UniProt 1–140 Author chain D； PDBConstruct 1–140； UniProt 1–140 Author chain E； PDBConstruct 1–140； UniProt 1–140 Author chain F； PDBConstruct 1–140； UniProt 1–140 Author chain G； PDBConstruct 1–140； UniProt 1–140 Author chain H； PDBConstruct 1–140； UniProt 1–140 Author chain I； PDBConstruct 1–140； UniProt 1–140 Author chain J； PDBConstruct 1–140； UniProt 1–140

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	2wcv
Deposition date deposition_date	2009-03-17
Structure title title	Crystal structure of bacterial FucU
Keywords keywords	RIBOSE, PYRANASE, ISOMERASE, FUCOSE METABOLISM; 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.

2wcv__assembly_2__model_1

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

Download this curve (.dat)

2wcv__assembly_2__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2wcv__assembly_2__model_1 | P(r) · Pending

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

Rg（Guinier）	34.98 Å
Rg (electron density)	33.69 Å
Total Rg	34.41 Å
Atom count	10990
Residues	1400
Excluded volume	199140 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2wcv__assembly_1__model_1`	decameric （10）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2wcv__assembly_2__model_1`	decameric （10）	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	L-FUCOSE MUTAROTASE
Molecular weight formula_weight	15490.1 kDa
EC 编号 ec_number	5.1.3.-
Source method src_method	man
Copy count entity_count	10

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D,E,F,G,H,I,J
Atom count atom_count	11306

MLKTISPLISPELLKVLAEMGHGDEIIFSDAHFPAHSMGPQVIRADGLLVSDLLQAIIPLFELDSYAPPLVMMAAVEGDTLDPEVERRYRNALSLQAPCPDIIRINRFAFYERAQKAFAIVITGERAKYGNILLKKGVTP

Source Source

Source organism organism	ESCHERICHIA COLI
NCBI taxonomy ID ncbi_taxonomy_id	562
Host organism host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 non-polymer

Description description	alpha-L-fucopyranose
Molecular weight formula_weight	164.2 kDa
Source method src_method	man
Copy count entity_count	10

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	356

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6. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (10 domains)

Domain ID domain_id	d2wcva_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.133 — RbsD-like
Superfamily Superfamily superfamily	c.133.1 — RbsD-like
Family Family family	c.133.1.0 — automated matches

Domain ID domain_id	d2wcvb_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.133 — RbsD-like
Superfamily Superfamily superfamily	c.133.1 — RbsD-like
Family Family family	c.133.1.0 — automated matches

Domain ID domain_id	d2wcvc_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.133 — RbsD-like
Superfamily Superfamily superfamily	c.133.1 — RbsD-like
Family Family family	c.133.1.0 — automated matches

Domain ID domain_id	d2wcvd_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.133 — RbsD-like
Superfamily Superfamily superfamily	c.133.1 — RbsD-like
Family Family family	c.133.1.0 — automated matches

Domain ID domain_id	d2wcve_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.133 — RbsD-like
Superfamily Superfamily superfamily	c.133.1 — RbsD-like
Family Family family	c.133.1.0 — automated matches

Domain ID domain_id	d2wcvf_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.133 — RbsD-like
Superfamily Superfamily superfamily	c.133.1 — RbsD-like
Family Family family	c.133.1.0 — automated matches

Domain ID domain_id	d2wcvg_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.133 — RbsD-like
Superfamily Superfamily superfamily	c.133.1 — RbsD-like
Family Family family	c.133.1.0 — automated matches

Domain ID domain_id	d2wcvh_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.133 — RbsD-like
Superfamily Superfamily superfamily	c.133.1 — RbsD-like
Family Family family	c.133.1.0 — automated matches

Domain ID domain_id	d2wcvi_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.133 — RbsD-like
Superfamily Superfamily superfamily	c.133.1 — RbsD-like
Family Family family	c.133.1.0 — automated matches

Domain ID domain_id	d2wcvj_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.133 — RbsD-like
Superfamily Superfamily superfamily	c.133.1 — RbsD-like
Family Family family	c.133.1.0 — automated matches

CATH v4.4 (10 domains)

Domain ID domain_id	2wcvA01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1650 — RbsD-like fold
Homologous superfamily homologous superfamily	10 — RbsD-like domain

Domain ID domain_id	2wcvB01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1650 — RbsD-like fold
Homologous superfamily homologous superfamily	10 — RbsD-like domain

Domain ID domain_id	2wcvC01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1650 — RbsD-like fold
Homologous superfamily homologous superfamily	10 — RbsD-like domain

Domain ID domain_id	2wcvD01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1650 — RbsD-like fold
Homologous superfamily homologous superfamily	10 — RbsD-like domain

Domain ID domain_id	2wcvE01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1650 — RbsD-like fold
Homologous superfamily homologous superfamily	10 — RbsD-like domain

Domain ID domain_id	2wcvF01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1650 — RbsD-like fold
Homologous superfamily homologous superfamily	10 — RbsD-like domain

Domain ID domain_id	2wcvG01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1650 — RbsD-like fold
Homologous superfamily homologous superfamily	10 — RbsD-like domain

Domain ID domain_id	2wcvH01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1650 — RbsD-like fold
Homologous superfamily homologous superfamily	10 — RbsD-like domain

Domain ID domain_id	2wcvI01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1650 — RbsD-like fold
Homologous superfamily homologous superfamily	10 — RbsD-like domain

Domain ID domain_id	2wcvJ01
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	1650 — RbsD-like fold
Homologous superfamily homologous superfamily	10 — RbsD-like domain

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Unit-cell length a length_a	131.976 Å
Unit-cell length b length_b	84.481 Å
Unit-cell length c length_c	113.076 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	92.02 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	40

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	1.900 Å
Low-resolution limit resolution_low	20.000 Å
R factor r_factor	0.1980
R_work r_work	0.1980
R_free r_free	0.2450

Crystal structure of bacterial FucU

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

L-FUCOSE MUTAROTASE

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

2wcv__assembly_2__model_1

2wcv__assembly_2__model_1 | I(q)

2wcv__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 (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) 20 domains

SCOP 2.08 (10 domains)

CATH v4.4 (10 domains)

7. Citations (1)

Crystal structure of bacterial FucU

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

L-FUCOSE MUTAROTASE

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

2wcv__assembly_2__model_1

2wcv__assembly_2__model_1 | I(q)

2wcv__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 (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) 20 domains

SCOP 2.08 (10 domains)

CATH v4.4 (10 domains)

7. Citations (1)