1eyr

Structure of a sialic acid activating synthetase, CMP acylneuraminate synthetase in the presence and absence of CDP

Method: X-RAY DIFFRACTION

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

CMP-N-ACETYLNEURAMINIC ACID SYNTHETASE

OrganismNot specified

UniProt P0A0Z8

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 CYTIDINE-5'-DIPHOSPHATE × 2 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name NEUA_NEIME
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–228; UniProt 1–228 Author chain B; PDBConstruct 1–228; UniProt 1–228

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.

2. Structure Basics 2. Structure Basics

Entry ID entry_id1eyr
Deposition date deposition_date2000-05-08
Structure title titleStructure of a sialic acid activating synthetase, CMP acylneuraminate synthetase in the presence and absence of CDP
Keywords keywordsSYNTHETASE, SIALIC ACID, CDP, ACYLNEURAMINATE, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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.

1eyr__assembly_1__model_1

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

Download this curve (.dat)

1eyr__assembly_1__model_1 | I(q)

10-2 10-1 105 106 107 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

1eyr__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)26.45 Å
Rg (electron density)26.11 Å
Total Rg26.76 Å
Atom count3452
Residues436
Excluded volume61461 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1eyr__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download

4. Crystallography and Experiment 4. Crystallography & Experiment

5. Entities and Polymers Entities & Polymers (3)

6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1eyra_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.68 — Nucleotide-diphospho-sugar transferases
Superfamily Superfamily superfamilyc.68.1 — Nucleotide-diphospho-sugar transferases
Family Family familyc.68.1.13 — Cytidylytransferase
Domain ID domain_idd1eyrb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.68 — Nucleotide-diphospho-sugar transferases
Superfamily Superfamily superfamilyc.68.1 — Nucleotide-diphospho-sugar transferases
Family Family familyc.68.1.13 — Cytidylytransferase

CATH v4.4 (2 domains)

Domain ID domain_id1eyrA00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology550 — Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
Homologous superfamily homologous superfamily10 — Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
Domain ID domain_id1eyrB00
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology550 — Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
Homologous superfamily homologous superfamily10 — Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

7. Citations (1)