Research workbench
The superhelical tpr domain of O-linked glcnac transferase reveals structural similarities to importin alpha.
Analyse The superhelical tpr domain of O-linked glcnac transferase reveals structural… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1W3B
- Type
- protein
- Length
- 756 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110
- EC
- 2.4.1.-
- UniProt
- O15294
- Ligands
- CA
- Pockets
- 3 · best druggability 0.47
Structure
x-ray diffraction · 2 distinct chains · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Udp-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 (EC 2.4.1.-) | protein | 388 | 75% helix, 0% strand | O15294 |
| B | Udp-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 (EC 2.4.1.-) | protein | 368 | 76% helix, 0% strand | O15294 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 107 | 0.47 | 0.79 | 19 | empty |
| 2 | 129 | 0.40 | 0.73 | 19 | empty |
| 3 | 62 | 0.36 | 0.78 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 556 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1W3B · The superhelical TPR domain of O-linked GlcNAc transferase reveals structural… · the same entry in another collection · chain A against A, TM-score 1.00
- O15294 · AlphaFold monomer V2.0 prediction for udp-N-acetylglucosamine-- peptide… · a predicted model of the same protein · chain A against A, TM-score 0.92
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 1W3B · PDBe 1W3B · UniProt O15294
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