Research workbench
Crystal structure of laminin BETA2 LE5-lf-LE6
Analyse Crystal structure of laminin BETA2 LE5-lf-LE6 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LF2
- Type
- protein
- Length
- 604 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Laminin subunit beta-2
- UniProt
- P15800
- Ligands
- CA, CL
- Pockets
- 9 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 15% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Laminin subunit beta-2 | protein | 302 | 15% helix, 31% strand | P15800 |
| B | Laminin subunit beta-2 | protein | 302 | 15% helix, 30% strand | P15800 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 415 | 0.57 | 0.74 | 37 | CL |
| 2 | 358 | 0.55 | 0.74 | 29 | CL |
| 3 | 116 | 0.45 | 0.78 | 17 | empty |
| 4 | 124 | 0.40 | 0.75 | 22 | empty |
| 5 | 90 | 0.36 | 0.75 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 743 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 disulfide (disulfide).
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 P15800
- Elsewhere: RCSB PDB 5LF2 · PDBe 5LF2 · UniProt P15800
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