Research workbench
Crystal structure of LIP5 N-terminal domain complexed with CHMP1B mim
Analyse Crystal structure of LIP5 N-terminal domain complexed with CHMP1B mim in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4TXQ
- Type
- protein
- Length
- 354 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vacuolar protein sorting-associated protein VTA1 homolog; Charged multivesicular body…
- UniProt
- Q9NP79, Q7LBR1
- Pockets
- 1 · best druggability 0.51
Structure
x-ray diffraction · 3 distinct chains · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Vacuolar protein sorting-associated protein VTA1 homolog | protein | 162 | 78% helix, 0% strand | Q9NP79 |
| C | Charged multivesicular body protein 1B | protein | 13 | 69% helix, 0% strand | Q7LBR1 |
| D | Charged multivesicular body protein 1B | protein | 17 | 82% helix, 0% strand | Q7LBR1 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 248 | 0.51 | 0.75 | 36 | empty |
Interfaces
3 interfaces between chains.
- B–D · 674 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 613 Ų buried · 13 hydrogen bonds · protein-protein
- A–C · 601 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 4TXQ · Crystal structure of LIP5 N-terminal domain complexed with CHMP1B MIM · the same entry in another collection · chain A against A, TM-score 1.00
- Q9NP79 · AlphaFold monomer V2.0 prediction for vacuolar protein sorting- associated protein VTA1… · a predicted model of the same protein · chain A against A, TM-score 0.97
- Q7LBR1 · AlphaFold monomer V2.0 prediction for charged multivesicular body protein 1B (Q7LBR1) · a predicted model of the same protein · chain C against A, TM-score 0.81
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9NP79
- Every structure of UniProt Q7LBR1
- Elsewhere: RCSB PDB 4TXQ · PDBe 4TXQ · UniProt Q9NP79 · UniProt Q7LBR1
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