Research workbench
Crystal structure of mouse alpha-1,4-N-acetylhexosaminyltransferase (EXTL2)
Analyse Crystal structure of mouse alpha-1,4-N-acetylhexosaminyltransferase (EXTL2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OMX
- Type
- protein
- Length
- 501 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-1,4-N-acetylhexosaminyltransferase EXTL2
- EC
- 2.4.1.-
- UniProt
- Q9ES89
- Pockets
- 6 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-1,4-N-acetylhexosaminyltransferase EXTL2 (EC 2.4.1.-) | protein | 250 | 31% helix, 26% strand | Q9ES89 |
| B | Alpha-1,4-N-acetylhexosaminyltransferase EXTL2 (EC 2.4.1.-) | protein | 251 | 29% helix, 26% strand | Q9ES89 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 272 | 0.56 | 0.77 | 45 | empty |
| 2 | 280 | 0.55 | 0.76 | 45 | empty |
| 3 | 103 | 0.48 | 0.80 | 22 | EDO |
| 4 | 78 | 0.31 | 0.74 | 18 | empty |
| 5 | 67 | 0.30 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1393 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1OMX · Crystal structure of mouse alpha-1,4-N-acetylhexosaminyltransferase (EXTL2) · the same entry in another collection · chain A against A, TM-score 1.00
- Q9ES89 · AlphaFold monomer V2.0 prediction for exostosin-like 2 (Q9ES89) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q9ES89
- Elsewhere: RCSB PDB 1OMX · PDBe 1OMX · UniProt Q9ES89
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.