Research workbench
Human pd-L1 bound to a macrocyclic peptide which blocks the pd-1/PD-L1 interaction
Analyse Human pd-L1 bound to a macrocyclic peptide which blocks the pd-1/PD-L1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PV9
- Type
- protein
- Length
- 220 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Programmed cell death 1 ligand 1; Macrocyclic peptide
- UniProt
- Q9NZQ7
- Ligands
- ACE, NH2
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Programmed cell death 1 ligand 1 | protein | 205 | 8% helix, 53% strand | Q9NZQ7 |
| B | Macrocyclic peptide | protein | 15 | 0% helix, 27% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 633 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified, 2 covalent, 2 disulfide, 1 d-amino (nonstandard, covalent ligand, disulfide, D-amino acid, methylation).
Compared structures
- 6PV9 · Human PD-L1 bound to a macrocyclic peptide which blocks the PD-1/PD-L1 interaction · 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 6PV9 · PDBe 6PV9 · UniProt Q9NZQ7
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