5jp2

Fcho1 Mu homology domain (Danio Rerio) with bound Eps15 peptide

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

Epidermal growth factor receptor substrate 15

Homo sapiens

UniProt P42566

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 2 F-BAR domain only protein 1 × 1 (A0A0R4IJ14) ZINC ION × 1 water × 2 Consistent with protein count
2 Protein heterocomplex Heteromer Protein 2 F-BAR domain only protein 1 × 1 (A0A0R4IJ14) water × 2 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name EPS15_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain E; PDBConstruct 1–23; UniProt 615–637 Author chain F; PDBConstruct 1–23; UniProt 615–637

F-BAR domain only protein 1

Danio rerio

UniProt A0A0R4IJ14

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 2 Epidermal growth factor receptor substrate 15 × 1 (P42566) ZINC ION × 1 water × 2 Consistent with protein count
2 Protein heterocomplex Heteromer Protein 2 Epidermal growth factor receptor substrate 15 × 1 (P42566) water × 2 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name A0A0R4IJ14_DANRE
Isoform —
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–286; UniProt 615–900 Author chain B; PDBConstruct 1–286; UniProt 615–900

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_id5jp2
Deposition date deposition_date2016-05-03
Structure title titleFcho1 Mu homology domain (Danio Rerio) with bound Eps15 peptide
Keywords keywordsFCHO Eps15 Mu homology domain Endocytosis, Signaling protein; SIGNALING PROTEIN
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.

5jp2__assembly_1__model_1

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

Download this curve (.dat)

5jp2__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.

5jp2__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)24.49 Å
Rg (electron density)23.62 Å
Total Rg24.32 Å
Atom count2229
Residues290
Excluded volume39468 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 5jp2__assembly_1__model_1 dimeric (2) Success 4.1.3-1-20251215 (887e7ef) View Download
2 1 5jp2__assembly_2__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 (4)

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7. Citations (1)