1exy

SOLUTION STRUCTURE OF HTLV-1 PEPTIDE BOUND TO ITS RNA APTAMER TARGET

Method: SOLUTION NMR

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

HTLV-1 REX PEPTIDE

OrganismNot specified

UniProt O56230

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein–RNA Monomer Protein 1 RNA 1 RNA APTAMER, 33-MER × 1 Consistent with all polymers

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name O56230_9DELA
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–16; UniProt 1–16

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_id1exy
Deposition date deposition_date2000-05-05
Structure title titleSOLUTION STRUCTURE OF HTLV-1 PEPTIDE BOUND TO ITS RNA APTAMER TARGET
Keywords keywords;arginine-guanine sandwich, extended bound basic Rex peptide, flap base, junctional base triplets, RNA binding pocket architecture, RNA BINDING PROTEIN-RNA COMPLEX ;; RNA BINDING PROTEIN/RNA
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.

1exy__assembly_1__model_7

Assembly 1 · Model 7 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

1exy__assembly_1__model_7 | I(q)

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

1exy__assembly_1__model_7 | 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)14.69 Å
Rg (electron density)14.10 Å
Total Rg14.90 Å
Atom count1382
Residues49
Excluded volume12537 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 1exy__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 2 1exy__assembly_1__model_2 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 3 1exy__assembly_1__model_3 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 4 1exy__assembly_1__model_4 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 5 1exy__assembly_1__model_5 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 6 1exy__assembly_1__model_6 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 7 1exy__assembly_1__model_7 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 8 1exy__assembly_1__model_8 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 9 1exy__assembly_1__model_9 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 10 1exy__assembly_1__model_10 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 11 1exy__assembly_1__model_11 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 12 1exy__assembly_1__model_12 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download

4. Crystallography and Experiment 4. Crystallography & Experiment

5. Entities and Polymers Entities & Polymers (2)

6. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1exyb_
Class classj — Peptides
Fold Fold foldj.9 — Arg-rich RNA binding peptides
Superfamily Superfamily superfamilyj.9.6 — HTLV-1 peptide
Family Family familyj.9.6.1 — HTLV-1 peptide

7. Citations (1)