MolNFT v1 · #128893 · protein
Structure of human pd-L1 in complex with inhibitor
5O45 · Programmed cell death 1 ligand 1: “Structure of human pd-L1 in complex with inhibitor”. X-ray diffraction, 1 ligand (NH2). MolNFT v1 #128893 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5O45
- Type
- protein
- Length
- 143 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Programmed cell death 1 ligand 1; Phe-mea-9KK-sar-asp-val-mea-tyr-sar-TRP-tyr-leu-ccs-gly…
- UniProt
- Q9NZQ7
- Ligands
- NH2
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Programmed cell death 1 ligand 1 | protein | 129 | 14% helix, 43% strand | Q9NZQ7 |
| B | Phe-mea-9KK-sar-asp-val-mea-tyr-sar-TRP-tyr-leu-ccs-gly- NH2 | protein | 14 | 0% helix, 0% strand | — |
Ligands and binding sites
- NH2 · Amino group · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 539 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified, 1 disulfide (nonstandard, methylation, disulfide).
Compared structures
- 5O45 · Structure of human PD-L1 in complex with inhibitor · 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 5O45 · PDBe 5O45 · UniProt Q9NZQ7
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