MolNFT v1 · #166335 · protein
High-affinity human pd-1 pd-L2 complex
6UMT: “High-affinity human pd-1 pd-L2 complex”. X-ray diffraction, 1 ligand (MG). MolNFT v1 #166335 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6UMT
- Type
- protein
- Length
- 208 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q15116, Q9BQ51
- Ligands
- MG
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 109 | — | Q15116 |
| B | — | protein | 99 | — | Q9BQ51 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6UMT · High-affinity human PD-1 PD-L2 complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q9BQ51 · AlphaFold monomer V2.0 prediction for programmed cell death 1 ligand 2 (Q9BQ51) · a predicted model of the same protein · chain B against A, TM-score 0.95
- Q15116 · AlphaFold monomer V2.0 prediction for programmed cell death protein 1 (Q15116) · a predicted model of the same protein · chain A against A, TM-score 0.93
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 Q15116
- Every structure of UniProt Q9BQ51
- Elsewhere: RCSB PDB 6UMT · PDBe 6UMT · UniProt Q15116 · UniProt Q9BQ51
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