MolNFT v1 · #97018 · protein
Crystal structure of mouse carmil residues 1-668
4K17 · Leucine-rich repeat-containing protein 16A: “Crystal structure of mouse carmil residues 1-668”. X-ray diffraction, 3 ligands (OHB, ABU, CL), 20 pockets (best druggability 0.77). MolNFT v1 #97018 on GenesisL1: 3D structure, binding…
- PDB
- 4K17
- Type
- protein
- Length
- 2,631 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Leucine-rich repeat-containing protein 16A
- UniProt
- Q6EDY6
- Ligands
- OHB, ABU, CL
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 4 distinct chains · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Leucine-rich repeat-containing protein 16A | protein | 660 | 42% helix, 16% strand | Q6EDY6 |
| B | Leucine-rich repeat-containing protein 16A | protein | 660 | 42% helix, 16% strand | Q6EDY6 |
| C | Leucine-rich repeat-containing protein 16A | protein | 656 | 43% helix, 16% strand | Q6EDY6 |
| D | Leucine-rich repeat-containing protein 16A | protein | 655 | 43% helix, 16% strand | Q6EDY6 |
Ligands and binding sites
- OHB · salicylamide · ligand · chains B
- ABU · Gamma-amino-butanoic acid · ligand · chains C
- CL · Chloride ion · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 87 | 0.77 | 0.97 | 19 | empty |
| 2 | 55 | 0.74 | 0.99 | 18 | empty |
| 3 | 126 | 0.73 | 0.91 | 20 | empty |
| 4 | 259 | 0.56 | 0.77 | 35 | empty |
| 5 | 253 | 0.54 | 0.77 | 30 | empty |
Interfaces
3 interfaces between chains.
- C–D · 1790 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 1746 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 161 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 72 modified, 2 disulfide (engineered, disulfide).
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 Q6EDY6
- Elsewhere: RCSB PDB 4K17 · PDBe 4K17 · UniProt Q6EDY6
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