Research workbench
Pd-1 binding domain from human pd-L1
Analyse Pd-1 binding domain from human pd-L1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5C3T
- Type
- protein
- Length
- 126 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Programmed cell death 1 ligand 1
- UniProt
- Q9NZQ7
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Programmed cell death 1 ligand 1 | protein | 126 | 17% helix, 45% strand | Q9NZQ7 |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5C3T · PD-1 binding domain from human 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 5C3T · PDBe 5C3T · UniProt Q9NZQ7
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