MolNFT v1 · #121654 · protein
Villin headpiece subdomain with a LYS30 to apc substitution
5I1S · Villin-1: “Villin headpiece subdomain with a LYS30 to apc substitution”. X-ray diffraction, 1 pocket (best druggability 0.49). MolNFT v1 #121654 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5I1S
- Type
- protein
- Length
- 140 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Villin-1; D-villin headpiece subdomain
- UniProt
- P02640
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 67% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Villin-1 | protein | 35 | 66% helix, 0% strand | P02640 |
| C, D | D-villin headpiece subdomain | protein | 35 | 69% helix, 0% strand | — |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 190 | 0.49 | 0.76 | 38 | empty |
Interfaces
5 interfaces between chains.
- B–D · 214 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 211 Ų buried · 4 hydrogen bonds · protein-protein
- A–C · 209 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 209 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 94 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 66 d-amino, 2 modified (D-amino acid, nonstandard).
Compared structures
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 P02640
- Elsewhere: RCSB PDB 5I1S · PDBe 5I1S · UniProt P02640
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