2yt1

Solution structure of the chimera of the C-terminal tail peptide of APP and the C-terminal PID domain of Fe65L

Method: SOLUTION NMR
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Amyloid beta A4 protein and Amyloid beta A4 precursor protein-binding family B member 2

Mus musculus

UniProt P12023

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Insufficient information 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 A4_MOUSE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 8–39; UniProt 739–770

Amyloid beta A4 protein and Amyloid beta A4 precursor protein-binding family B member 2

Mus musculus

UniProt Q9DBR4

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Insufficient information 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 APBB2_MOUSE
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 63–185; UniProt 582–704

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_id2yt1
Deposition date deposition_date2007-04-05
Structure title titleSolution structure of the chimera of the C-terminal tail peptide of APP and the C-terminal PID domain of Fe65L
Keywords keywords;Chimera, Fe65L, PID domain, amyloid precursor protein, Structural Genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI, PROTEIN BINDING ;; PROTEIN BINDING
Experimental Method methodSOLUTION NMR
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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.

2yt1__assembly_1__model_1

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

Download this curve (.dat)

2yt1__assembly_1__model_1 | I(q)

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

2yt1__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)20.94 Å
Rg (electron density)19.79 Å
Total Rg20.61 Å
Atom count2718
Residues185
Excluded volume24368 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 2yt1__assembly_1__model_1 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 2 2yt1__assembly_1__model_2 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 3 2yt1__assembly_1__model_3 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 4 2yt1__assembly_1__model_4 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 5 2yt1__assembly_1__model_5 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 6 2yt1__assembly_1__model_6 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 7 2yt1__assembly_1__model_7 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 8 2yt1__assembly_1__model_8 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 9 2yt1__assembly_1__model_9 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 10 2yt1__assembly_1__model_10 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 11 2yt1__assembly_1__model_11 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 12 2yt1__assembly_1__model_12 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 13 2yt1__assembly_1__model_13 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 14 2yt1__assembly_1__model_14 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 15 2yt1__assembly_1__model_15 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 16 2yt1__assembly_1__model_16 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 17 2yt1__assembly_1__model_17 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 18 2yt1__assembly_1__model_18 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 19 2yt1__assembly_1__model_19 monomeric (1) Success 4.1.3-1-20251215 (887e7ef) View Download
1 20 2yt1__assembly_1__model_20 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 (1)

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6. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id2yt1A01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology29 — PH-domain like
Homologous superfamily homologous superfamily30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
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7. Citations (1)