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Crystal structure of the pd-L1
Analyse Crystal structure of the pd-L1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BIS
- Type
- protein
- Length
- 424 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Programmed cell death 1 ligand 1
- UniProt
- Q9NZQ7
- Pockets
- 4 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Programmed cell death 1 ligand 1 | protein | 212 | 5% helix, 54% strand | Q9NZQ7 |
| B | Programmed cell death 1 ligand 1 | protein | 212 | 6% helix, 53% strand | Q9NZQ7 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 590 | 0.70 | 0.79 | 56 | empty |
| 2 | 394 | 0.60 | 0.76 | 31 | empty |
| 3 | 142 | 0.47 | 0.78 | 25 | empty |
| 4 | 94 | 0.35 | 0.74 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1013 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 3BIS · Crystal Structure of the PD-L1 · 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 Q9NZQ7
- Elsewhere: RCSB PDB 3BIS · PDBe 3BIS · UniProt Q9NZQ7
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