MolNFT v1 · #85912 · protein
Laminin BETA1 ln-LE1-4 structure
4AQS · Laminin subunit beta-1: “Laminin BETA1 ln-LE1-4 structure”. X-ray diffraction, 4 ligands (NAG, BMA, MAN), 1 pocket (best druggability 0.45). MolNFT v1 #85912 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4AQS
- Type
- protein
- Length
- 453 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Laminin subunit beta-1
- UniProt
- P02469
- Ligands
- NAG, BMA, MAN, FUL
- Pockets
- 1 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Laminin subunit beta-1 | protein | 453 | 7% helix, 28% strand | P02469 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
- BMA · beta-D-mannopyranose · sugar
- MAN · alpha-D-mannopyranose · sugar
- FUL · beta-L-fucopyranose · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 164 | 0.45 | 0.75 | 21 | empty |
Modifications
Observed in the structure: 19 disulfide, 2 glycan (disulfide, N-glycosylation).
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 P02469
- Elsewhere: RCSB PDB 4AQS · PDBe 4AQS · UniProt P02469
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