MolNFT v1 · #106658 · protein
Crystal structure of SEC14-like protein 4 (SEC14L4)
4TLG: “Crystal structure of SEC14-like protein 4 (SEC14L4)”. X-ray diffraction, 1 ligand (11A), 13 pockets (best druggability 0.83). MolNFT v1 #106658 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4TLG
- Type
- protein
- Length
- 784 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SEC14-like protein 4
- UniProt
- Q9UDX3
- Ligands
- 11A
- Pockets
- 13 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SEC14-like protein 4 | protein | 396 | 37% helix, 23% strand | Q9UDX3 |
| B | SEC14-like protein 4 | protein | 388 | 40% helix, 24% strand | Q9UDX3 |
Ligands and binding sites
- 11A · Undecanoic acid · ligand · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 26 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 196 | 0.83 | 0.96 | 26 | 11A |
| 2 | 178 | 0.83 | 0.97 | 26 | 11A |
| 3 | 66 | 0.71 | 0.96 | 23 | EDO |
| 4 | 124 | 0.59 | 0.85 | 24 | EDO |
| 5 | 267 | 0.53 | 0.75 | 27 | EDO |
Interfaces
1 interface between chains.
- A–B · 145 Ų buried · 2 hydrogen bonds · protein-protein
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 Q9UDX3
- Elsewhere: RCSB PDB 4TLG · PDBe 4TLG · UniProt Q9UDX3
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.