Research workbench
Cryo-EM structure of unliganded O-glcnac transferase
Analyse Cryo-EM structure of unliganded O-glcnac transferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NTF
- Type
- protein
- Length
- 1,740 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Isoform 1 of udp-N-acetylglucosamine--peptide N- acetylglucosaminyltransferase 110 kda…
- EC
- 2.4.1.255
- UniProt
- O15294
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 2 distinct chains · 59% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Isoform 1 of udp-N-acetylglucosamine--peptide N- acetylglucosaminyltransferase 110 kda subunit (EC 2.4.1.255) | protein | 918 | 60% helix, 8% strand | O15294 |
| B | Isoform 1 of udp-N-acetylglucosamine--peptide N- acetylglucosaminyltransferase 110 kda subunit (EC 2.4.1.255) | protein | 822 | 58% helix, 9% strand | O15294 |
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 768 | 0.83 | 0.86 | 148 | empty |
| 2 | 478 | 0.79 | 0.87 | 105 | empty |
| 3 | 637 | 0.79 | 0.84 | 84 | empty |
| 4 | 344 | 0.75 | 0.86 | 64 | empty |
| 5 | 473 | 0.74 | 0.83 | 62 | empty |
Interfaces
1 interface between chains.
- A–B · 77 Ų buried · 0 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 O15294
- Elsewhere: RCSB PDB 7NTF · PDBe 7NTF · UniProt O15294
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