Research workbench
Yeast BBC1 SH3 domain complexed with a peptide from LAS17
Analyse Yeast BBC1 SH3 domain complexed with a peptide from LAS17 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZUK
- Type
- protein
- Length
- 141 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Myosin tail region-interacting protein MTI1; Proline-rich protein LAS17
- UniProt
- P47068, Q12446
- Ligands
- MG, CL
- Pockets
- 1 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Myosin tail region-interacting protein MTI1 | protein | 65 | 5% helix, 49% strand | P47068 |
| C | Proline-rich protein LAS17 | protein | 11 | 0% helix, 0% strand | Q12446 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 136 | 0.61 | 0.85 | 32 | CL |
Interfaces
3 interfaces between chains.
- A–C · 430 Ų buried · 4 hydrogen bonds · protein-protein
- B–C · 412 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 238 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1ZUK · Yeast BBC1 Sh3 domain complexed with a peptide from Las17 · the same entry in another collection · chain A against A, TM-score 1.00
- P47068 · AlphaFold monomer V2.0 prediction for myosin tail region-interacting protein MTI1 (P47068) · a predicted model of the same protein · chain B against A, TM-score 0.97
- Q12446 · AlphaFold monomer V2.0 prediction for proline-rich protein LAS17 (Q12446) · a predicted model of the same protein · chain C against A, TM-score 0.53
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 P47068
- Every structure of UniProt Q12446
- Elsewhere: RCSB PDB 1ZUK · PDBe 1ZUK · UniProt P47068 · UniProt Q12446
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