Research workbench
N-acetylhexosamine 1-phosphate kinase in complex with galnac
Analyse N-acetylhexosamine 1-phosphate kinase in complex with galnac in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OCQ
- Type
- protein
- Length
- 355 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acetylhexosamine 1-phosphate kinase
- EC
- 2.7.1.162
- UniProt
- T2I3Q3
- Ligands
- A2G
- Pockets
- 4 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetylhexosamine 1-phosphate kinase (EC 2.7.1.162) | protein | 355 | 49% helix, 14% strand | T2I3Q3 |
Ligands and binding sites
- A2G · 2-acetamido-2-deoxy-alpha-D-galactopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 356 | 0.79 | 0.89 | 49 | A2G |
| 2 | 92 | 0.45 | 0.80 | 18 | empty |
| 3 | 78 | 0.42 | 0.79 | 17 | empty |
| 4 | 79 | 0.39 | 0.77 | 16 | empty |
Compared structures
- 4OCQ · N-acetylhexosamine 1-phosphate kinase in complex with GalNAc · the same entry in another collection · chain A against A, TM-score 1.00
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 T2I3Q3
- Elsewhere: RCSB PDB 4OCQ · PDBe 4OCQ · UniProt T2I3Q3
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