5i22

Amphiphysin SH3 in complex with Chikungunya virus nsP3 peptide

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

Myc box-dependent-interacting protein 1

Homo sapiens

UniProt O00499

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 2 CHIKV nsP3 peptide × 1 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name BIN1_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–81; UniProt 513–593

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_id5i22
Deposition date deposition_date2016-02-04
Structure title titleAmphiphysin SH3 in complex with Chikungunya virus nsP3 peptide
Keywords keywordsSH3 domain, function: protein binding Chikungunya virus nsP3 peptide, function: viral replication, Transcription; TRANSCRIPTION
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.

5i22__assembly_1__model_1

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

Download this curve (.dat)

5i22__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.

5i22__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)15.43 Å
Rg (electron density)14.18 Å
Total Rg15.50 Å
Atom count1569
Residues98
Excluded volume13974 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 5i22__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 2 5i22__assembly_1__model_2 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 3 5i22__assembly_1__model_3 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 4 5i22__assembly_1__model_4 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 5 5i22__assembly_1__model_5 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 6 5i22__assembly_1__model_6 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 7 5i22__assembly_1__model_7 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 8 5i22__assembly_1__model_8 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 9 5i22__assembly_1__model_9 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 10 5i22__assembly_1__model_10 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 11 5i22__assembly_1__model_11 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 12 5i22__assembly_1__model_12 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 13 5i22__assembly_1__model_13 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 14 5i22__assembly_1__model_14 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 15 5i22__assembly_1__model_15 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 16 5i22__assembly_1__model_16 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 17 5i22__assembly_1__model_17 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 18 5i22__assembly_1__model_18 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 19 5i22__assembly_1__model_19 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
1 20 5i22__assembly_1__model_20 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 (2)

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6. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd5i22a_
Class classb — All beta proteins
Fold Fold foldb.34 — SH3-like barrel
Superfamily Superfamily superfamilyb.34.2 — SH3-domain
Family Family familyb.34.2.1 — SH3-domain

CATH v4.4 (1 domains)

Domain ID domain_id5i22A00
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology30 — SH3 type barrels.
Homologous superfamily homologous superfamily40 — SH3 Domains
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7. Citations (1)