Research workbench
Thermostabilised human A2A receptor with neca bound
Analyse Thermostabilised human A2A receptor with neca bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YDV
- Type
- protein
- Length
- 315 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenosine receptor A2A
- UniProt
- P29274
- Ligands
- SOG, NEC
- Pockets
- 3 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 77% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenosine receptor A2A | protein | 315 | 77% helix, 1% strand | P29274 |
Ligands and binding sites
- SOG · octyl 1-thio-beta-D-glucopyranoside · ligand · 5 copies · chains A
- NEC · N-ethyl-5'-carboxamido adenosine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 295 | 0.75 | 0.87 | 35 | NEC |
| 2 | 201 | 0.49 | 0.75 | 23 | empty |
| 3 | 71 | 0.36 | 0.76 | 16 | empty |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
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 P29274
- Elsewhere: RCSB PDB 2YDV · PDBe 2YDV · UniProt P29274
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