1vlt

LIGAND BINDING DOMAIN OF THE WILD-TYPE ASPARTATE RECEPTOR WITH ASPARTATE

Method: X-RAY DIFFRACTION
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1. Protein Identity and Related Structures Protein Identity & Related Structures

ASPARTATE RECEPTOR

Salmonella typhimurium

UniProt P02941

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein homooligomer Homooligomer Protein 2 ASPARTIC ACID × 2 water × 2 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name MCP2_SALTY
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–146; UniProt 36–180 Author chain B; PDBConstruct 2–146; UniProt 36–180

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_id1vlt
Deposition date deposition_date1996-09-17
Structure title titleLIGAND BINDING DOMAIN OF THE WILD-TYPE ASPARTATE RECEPTOR WITH ASPARTATE
Keywords keywordsCOMPLEX (CHEMOTAXIS-PEPTIDE), CHEMOTAXIS, BACTERIAL CHEMOTAXIS RECEPTOR, BOUND, COMPLEX (CHEMOTAXIS-PEPTIDE) complex; COMPLEX (CHEMOTAXIS/PEPTIDE)
Experimental Method methodX-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.

1vlt__assembly_1__model_1

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

Download this curve (.dat)

1vlt__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.

1vlt__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)20.82 Å
Rg (electron density)20.05 Å
Total Rg20.88 Å
Atom count2247
Residues285
Excluded volume39349 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1vlt__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 (3)

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6. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1vlta_
Class classa — All alpha proteins
Fold Fold folda.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamilya.24.2 — Aspartate receptor, ligand-binding domain
Family Family familya.24.2.1 — Aspartate receptor, ligand-binding domain
Domain ID domain_idd1vltb_
Class classa — All alpha proteins
Fold Fold folda.24 — Four-helical up-and-down bundle
Superfamily Superfamily superfamilya.24.2 — Aspartate receptor, ligand-binding domain
Family Family familya.24.2.1 — Aspartate receptor, ligand-binding domain

CATH v4.4 (2 domains)

Domain ID domain_id1vltA00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily30 — Aspartate receptor, ligand-binding domain
Domain ID domain_id1vltB00
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology120 — Four Helix Bundle (Hemerythrin (Met), subunit A)
Homologous superfamily homologous superfamily30 — Aspartate receptor, ligand-binding domain
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7. Citations (3)