Research workbench
HA17-HA33-lacnac
Analyse HA17-HA33-lacnac in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LO3
- Type
- protein
- Length
- 715 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ha-33; Ha-17
- UniProt
- Q45871, Q45878
- Ligands
- NDG, GAL
- Pockets
- 7 · best druggability 0.48
Structure
x-ray diffraction · 3 distinct chains · 9% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ha-33 | protein | 286 | 10% helix, 47% strand | Q45871 |
| C | Ha-17 | protein | 144 | 6% helix, 52% strand | Q45878 |
| B | Ha-33 | protein | 285 | 8% helix, 47% strand | Q45871 |
Ligands and binding sites
- NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar · 2 copies · chains A, B
- GAL · beta-D-galactopyranose · sugar · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 155 | 0.48 | 0.78 | 26 | empty |
| 2 | 116 | 0.43 | 0.78 | 20 | empty |
| 3 | 101 | 0.43 | 0.77 | 23 | empty |
| 4 | 61 | 0.39 | 0.80 | 11 | empty |
| 5 | 79 | 0.31 | 0.73 | 16 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1005 Ų buried · 14 hydrogen bonds · protein-protein
- C–B · 710 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 452 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 4LO3 · HA17-HA33-LacNac · 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 Q45871
- Every structure of UniProt Q45878
- Elsewhere: RCSB PDB 4LO3 · PDBe 4LO3 · UniProt Q45871 · UniProt Q45878
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