MolNFT v1 · #173257 · protein
Cryo-EM structure of human exostosin-like 3 (EXTL3)
7AU2: “Cryo-EM structure of human exostosin-like 3 (EXTL3)”. Electron microscopy, 3 ligands (NAG, BMA, MAN), 20 pockets (best druggability 0.86). MolNFT v1 #173257 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7AU2
- Type
- protein
- Length
- 1,372 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Exostosin-like 3
- EC
- 2.4.1.223
- UniProt
- O43909
- Ligands
- NAG, BMA, MAN
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 1 distinct chain · 34% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Exostosin-like 3 (EC 2.4.1.223) | protein | 686 | 34% helix, 17% strand | O43909 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar · 2 copies · chains A, B
- MAN · alpha-D-mannopyranose · sugar · 2 copies · chains A, 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, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 860 | 0.86 | 0.88 | 115 | empty |
| 2 | 1131 | 0.82 | 0.83 | 69 | empty |
| 3 | 598 | 0.79 | 0.85 | 58 | empty |
| 4 | 132 | 0.74 | 0.94 | 24 | empty |
| 5 | 123 | 0.74 | 0.94 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 4769 Ų buried · 58 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide, 4 glycan (disulfide, N-glycosylation).
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 O43909
- Elsewhere: RCSB PDB 7AU2 · PDBe 7AU2 · UniProt O43909
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