Research workbench
GLUR0 ligand binding core complex with L-serine
Analyse GLUR0 ligand binding core complex with L-serine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1IIT
- Type
- protein
- Length
- 221 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SLR1257 protein
- UniProt
- P73797
- Ligands
- SER
- Pockets
- 1 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SLR1257 protein | protein | 221 | 38% helix, 28% strand | P73797 |
Ligands and binding sites
- SER · Serine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 201 | 0.62 | 0.82 | 36 | SER |
Compared structures
- 1IIT · GLUR0 ligand binding core complex with L-serine · 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 P73797
- Elsewhere: RCSB PDB 1IIT · PDBe 1IIT · UniProt P73797
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