SAXSdb — 2yqj

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

UDP-N-acetylglucosamine pyrophosphorylase

Candida albicans

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein monomer	Monomer	Protein 1	SULFATE ION × 2 MAGNESIUM ION × 1 URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE × 1 GLYCEROL × 1 water × 1	Consistent with protein count
2	Protein monomer	Monomer	Protein 1	SULFATE ION × 1 URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE × 1 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	UAP1_CANAL
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–486； UniProt 1–486 Author chain B； PDBConstruct 1–486； 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	2yqj
Deposition date deposition_date	2007-03-30
Structure title title	Crystal Structure of uridine-diphospho-N-acetylglucosamine pyrophosphorylase from Candida albicans, in the reaction-completed form
Keywords keywords	Pyrophosphorylase, N-acetylglucosamine, uridine-diphospho-N-acetylglucosamine, Candida albicans, TRANSFERASE; TRANSFERASE
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.

2yqj__assembly_1__model_1

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

Download this curve (.dat)

2yqj__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

2yqj__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	24.43 Å
Rg (electron density)	23.45 Å
Total Rg	24.20 Å
Atom count	3719
Residues	473
Excluded volume	66164 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`2yqj__assembly_1__model_1`	monomeric （1）	Success	4.1.3-1-20251215 (887e7ef)	View Download
2	1	`2yqj__assembly_2__model_1`	monomeric （1）	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 (6)

Entity 1 Entity 1 polymer

Description description	UDP-N-acetylglucosamine pyrophosphorylase
Molecular weight formula_weight	54727.8 kDa
EC 编号 ec_number	2.7.7.23
Mutation mutation	S216L
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	7615

MTVKSQQQIIDSFKQANQDQLFQYYDSLTIDQQQEFIDQLSTIEEPAKLISTVEQAIQFSQTNSTSRNFTQLPNEQTASTLDLSKDILQNWTELGLKAIGNGEVAVLLMAGGQGTRLGSSAPKGCFNIELPSQKSLFQIQAEKILKIEQLAQQYLKSTKKPIINWYIMTSGPTRNATESFFIENNYFGLNSHQVIFFNQGTLPCFNLQGNKILLELKNSICQSPDGNGGLYKALKDNGILDDLNSKGIKHIHMYCVDNCLVKVADPIFIGFAIAKKFDLATKVVRKRDANESVGLIVLDQDNQKPCVIEYSEISQELANKKDPQDSSKLFLRAANIVNHYYSVEFLNKMIPKWISSQKYLPFHIAKKKIPSLNLENGEFYKPTEPNGIKLEQFIFDVFPSVELNKFGCLEVDRLDEFSPLKNADGAKNDTPTTCRNHYLERSSKWVIQNGGVIDNQGLVEVDSKTSYGGEGLEFVNGKHFKNGDII

Source Source

Source organism organism	Candida albicans
NCBI taxonomy ID ncbi_taxonomy_id	5476
Host organism host_organism	Escherichia coli

Entity 2 Entity 2 non-polymer

Description description	SULFATE ION
Molecular weight formula_weight	96.1 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 3 Entity 3 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 non-polymer

Description description	URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE
Molecular weight formula_weight	607.4 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 non-polymer

Description description	GLYCEROL
Molecular weight formula_weight	92.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	223

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d2yqja_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.68 — Nucleotide-diphospho-sugar transferases
Superfamily Superfamily superfamily	c.68.1 — Nucleotide-diphospho-sugar transferases
Family Family family	c.68.1.0 — automated matches

Domain ID domain_id	d2yqjb_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.68 — Nucleotide-diphospho-sugar transferases
Superfamily Superfamily superfamily	c.68.1 — Nucleotide-diphospho-sugar transferases
Family Family family	c.68.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id	2yqjA01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	550 — Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
Homologous superfamily homologous superfamily	10 — Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Domain ID domain_id	2yqjB01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	550 — Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
Homologous superfamily homologous superfamily	10 — Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

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Unit-cell length a length_a	47.556 Å
Unit-cell length b length_b	61.975 Å
Unit-cell length c length_c	90.249 Å
Unit-cell angle α angle_alpha	90.07 °
Unit-cell angle β angle_beta	98.11 °
Unit-cell angle γ angle_gamma	92.93 °
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	2.310 Å
Low-resolution limit resolution_low	47.020 Å
R factor r_factor	0.1930
R_work r_work	0.1930
R_free r_free	0.2370

Crystal Structure of uridine-diphospho-N-acetylglucosamine pyrophosphorylase from Candida albicans, in the reaction-completed form

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

UDP-N-acetylglucosamine pyrophosphorylase

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

2yqj__assembly_1__model_1

2yqj__assembly_1__model_1 | I(q)

2yqj__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 (6)

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 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)

Crystal Structure of uridine-diphospho-N-acetylglucosamine pyrophosphorylase from Candida albicans, in the reaction-completed form

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

UDP-N-acetylglucosamine pyrophosphorylase

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

2yqj__assembly_1__model_1

2yqj__assembly_1__model_1 | I(q)

2yqj__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 (6)

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 non-polymer

Entity 6 Entity 6 water

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

CATH v4.4 (2 domains)

7. Citations (1)