6VME: Human ESCRT-I heterotetramer headpiece
Human ESCRT-I heterotetramer headpiece. Determined by X-ray diffraction at 2.19 Å resolution. Released 20 May 2020.
- Method
- X-ray diffraction
- Resolution
- 2.19 Å
- Organism
- Homo sapiens
- Chains
- 24
- Atoms
- 12,786
- Mol. weight
- 204.22 kDa
- Released
- 20 May 2020
Explore 6VME in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6VME contains 69 α-helices and 12 β-strands across 24 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
Chains A, D and R: 2 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 208-210 | 3 | |
| α-helix | 212-215 | 4 | |
| β-strand | 220-222 | 3 | 5 |
Chain B: 3 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 314-316 | 3 | |
| β-strand | 318-320 | 3 | 1 |
| α-helix | 323-350 | 28 | |
| α-helix | 356-383 | 28 | |
Chains C and K: 2 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 103-129 | 27 | |
| α-helix | 135-162 | 28 | |
Chains E, U and Y: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 30-57 | 28 | |
| α-helix | 63-84 | 22 | |
| α-helix | 92-98 | 7 | |
| α-helix | 104-112 | 9 | |
Chain F: 3 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 314-317 | 4 | |
| β-strand | 318-320 | 3 | 2 |
| α-helix | 323-350 | 28 | |
| α-helix | 356-384 | 29 | |
Chain G: 2 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 318-320 | 3 | 3 |
| α-helix | 323-350 | 28 | |
| α-helix | 356-383 | 28 | |
Chain H: 3 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 314-317 | 4 | |
| β-strand | 318-320 | 3 | 4 |
| α-helix | 323-350 | 28 | |
| α-helix | 356-383 | 28 | |
Chain I: 2 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 318-320 | 3 | 5 |
| α-helix | 323-350 | 28 | |
| α-helix | 356-384 | 29 | |
10 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Tumor susceptibility gene 101 protein | B, F, G, H, I, J | protein | 81 | Homo sapiens | Q99816 (AlphaFold model) |
| Vacuolar protein sorting-associated protein 37B | C, K, L, M, N, O | protein | 71 | Homo sapiens | Q9H9H4 (AlphaFold model) |
| Multivesicular body subunit 12A | A, D, P, Q, R, T | protein | 25 | Homo sapiens | Q96EY5 (AlphaFold model) |
| Vacuolar protein sorting-associated protein 28 homolog | E, U, V, W, X, Y | protein | 122 | Homo sapiens | Q9UK41 (AlphaFold model) |
Sequence of entity 1 (B, F, G, H, I, J), FASTA
>6VME_1 Tumor susceptibility gene 101 protein (chains B, F, G, H, I, J)
QSENNDIDEVIIPTAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKHVRLLS
RKQFQLRALMQKARKTAGLSD
Sequence of entity 2 (C, K, L, M, N, O), FASTA
>6VME_2 Vacuolar protein sorting-associated protein 37B (chains C, K, L, M, N, O)
QSSSASLETLLALLQAEGAKIEEDTENMAEKFLDGELPLDSFIDVYQSKRKLAHMRRVKI
EKLQEMVLKGQ
Sequence of entity 3 (A, D, P, Q, R, T), FASTA
>6VME_3 Multivesicular body subunit 12A (chains A, D, P, Q, R, T)
SNASSLYGISAMDGVPFTLHPRFEG
Sequence of entity 4 (E, U, V, W, X, Y), FASTA
>6VME_4 Vacuolar protein sorting-associated protein 28 homolog (chains E, U, V, W, X, Y)
MFHGIPATPGIGAPGNKPELYEEVKLYKNAREREKYDNMAELFAVVKTMQALEKAYIKDC
VSPSEYTAACSRLLVQYKAAFRQVQGSEISSIDEFCRKFRLDCPLAMERIKEDRPITIKD
DK
Primary citation
A helical assembly of human ESCRT-I scaffolds reverse-topology membrane scission. Flower, T.G., Takahashi, Y., Hudait, A. et al. Nat Struct Mol Biol (2020) 27:570-580. DOI 10.1038/s41594-020-0426-4 · PubMed
Other PDB entries of the same protein (UniProt Q99816 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7NLC 1.4 Å, Crystallographic structure of human Tsg101 UEV domain in complex with a HEV ORF3 peptide
- 3OBQ 1.4 Å, Crystal Structure of the Tsg101 UEV domain in complex with a human HRS PSAP peptide
- 3OBS 1.5 Å, Crystal structure of Tsg101 UEV domain
- 3OBU 1.6 Å, Crystal structure of the Tsg101 UEV domain in complex with a HIV-1 PTAP peptide
- 3OBX 1.6 Å, Crystal structure of the Tsg101 UEV domain in complex with a HIV-1 Gag P7A mutant peptide
- 3P9G 1.8 Å, Crystal structure of the TSG101 UEV domain in complex with FA459 peptide
- 3P9H 1.8 Å, Crystal structure of the TSG101 UEV domain in complex with FA258 peptide
- 1S1Q 2.0 Å, TSG101(UEV) domain in complex with Ubiquitin
- 4YC1 2.0 Å, Structure of the human TSG101-UEV domain in the P321 space group
- 4EJE 2.2 Å, Structure Of The Tsg101 UEV Domain In Complex With an Ebola PTAP late Domain Peptide
- 7ZLX 2.25 Å, Crystal Structure of the TSG101-UEV domain:space group P21
- 2F0R 2.26 Å, Crystallographic structure of human Tsg101 UEV domain
Browse structure collections
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