1df3

SOLUTION STRUCTURE OF A RECOMBINANT MOUSE MAJOR URINARY PROTEIN

Method: SOLUTION NMR
▼

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

MAJOR URINARY PROTEIN

Mus musculus

UniProt P11589

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein monomer Monomer Protein 1 No other associated polymer Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name MUP2_MOUSE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–162; UniProt 19–180

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id1df3
Deposition date deposition_date1999-11-17
Structure title titleSOLUTION STRUCTURE OF A RECOMBINANT MOUSE MAJOR URINARY PROTEIN
Keywords keywords;LIPOCALIN, CARRIER PROTEIN, PHEROMONE, 8-STRANDED BETA-BARREL, BINDING POCKET, DISULFIDE BRIDGE (64-157), SIGNALING PROTEIN, TRANSPORT PROTEIN ;; TRANSPORT PROTEIN
Experimental Method methodSOLUTION NMR
▼

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.

1df3__assembly_1__model_9

Assembly 1 · Model 9 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1df3__assembly_1__model_9 | I(q)

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

1df3__assembly_1__model_9 | 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)16.98 Å
Rg (electron density)15.37 Å
Total Rg16.55 Å
Atom count2601
Residues162
Excluded volume23099 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1df3__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 2 1df3__assembly_1__model_2 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 3 1df3__assembly_1__model_3 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 4 1df3__assembly_1__model_4 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 5 1df3__assembly_1__model_5 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 6 1df3__assembly_1__model_6 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 7 1df3__assembly_1__model_7 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 8 1df3__assembly_1__model_8 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 9 1df3__assembly_1__model_9 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 10 1df3__assembly_1__model_10 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (1)

▼

6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1df3a_
Class classb — All beta proteins
Fold Fold foldb.60 — Lipocalins
Superfamily Superfamily superfamilyb.60.1 — Lipocalins
Family Family familyb.60.1.1 — Retinol binding protein-like

CATH v4.4 (1 domains)

Domain ID domain_id1df3A00
Class class2 — Mainly Beta
Architecture architecture40 — Beta Barrel
Topology topology128 — Lipocalin
Homologous superfamily homologous superfamily20 — Calycin beta-barrel core domain
▶

7. Citations (3)