Research workbench
Crystal structure of the extracellular domain of murine pd-1
Analyse Crystal structure of the extracellular domain of murine pd-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NPU
- Type
- protein
- Length
- 116 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Programmed cell death protein 1
- UniProt
- Q02242
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Programmed cell death protein 1 | protein | 116 | 3% helix, 56% strand | Q02242 |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1NPU · Crystal structure of the extracellular domain of murine pd-1 · the same entry in another collection · chain A against A, TM-score 1.00
- Q02242 · AlphaFold monomer V2.0 prediction for programmed cell death protein 1 (Q02242) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q02242
- Elsewhere: RCSB PDB 1NPU · PDBe 1NPU · UniProt Q02242
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