3um1

Crystal structure of the Brox Bro1 domain in complex with the C-terminal tail of CHMP5

Method: X-RAY DIFFRACTION
▼

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

BRO1 domain-containing protein BROX

Homo sapiens

UniProt Q5VW32

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 Charged multivesicular body protein 5 × 2 (Q9NZZ3) GLYCEROL × 1 water × 4 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name BROX_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–376; UniProt 2–377 Author chain D; PDBConstruct 1–376; UniProt 2–377

Charged multivesicular body protein 5

Homo sapiens

UniProt Q9NZZ3

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 4 BRO1 domain-containing protein BROX × 2 (Q5VW32) GLYCEROL × 1 water × 4 Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name CHMP5_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–69; UniProt 151–219 Author chain E; PDBConstruct 1–69; UniProt 151–219

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_id3um1
Deposition date deposition_date2011-11-11
Structure title titleCrystal structure of the Brox Bro1 domain in complex with the C-terminal tail of CHMP5
Keywords keywordsbeta hairpin, ESCRT-III, CHMPs, MEMBRANE PROTEIN-TRANSPORT PROTEIN complex, BROX; MEMBRANE PROTEIN/TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION
▼

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.

3um1__assembly_1__model_1

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

Download this curve (.dat)

3um1__assembly_1__model_1 | I(q)

10-2 10-1 105 106 107 108 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

3um1__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)44.71 Å
Rg (electron density)45.97 Å
Total Rg45.66 Å
Atom count6244
Residues784
Excluded volume111620 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 3um1__assembly_1__model_1 tetrameric (4) Success 4.1.3-1-20251215 (887e7ef) View Download
▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (4)

▼

6. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id3um1A00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily280 — alix/aip1 like domains
Domain ID domain_id3um1D00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily280 — alix/aip1 like domains
▶

7. Citations (1)