MolNFT v1 · #97705 · protein
Human folate receptor beta (FOLR2) at neutral pH
4KMY: “Human folate receptor beta (FOLR2) at neutral pH”. X-ray diffraction, 2 ligands (NAG, K), 1 pocket (best druggability 0.67). MolNFT v1 #97705 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4KMY
- Type
- protein
- Length
- 207 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Folate receptor beta
- UniProt
- P14207
- Ligands
- NAG, K
- Pockets
- 1 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Folate receptor beta | protein | 207 | 32% helix, 13% strand | P14207 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
- K · Potassium ion · metal · 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 | 291 | 0.67 | 0.82 | 33 | empty |
Modifications
Observed in the structure: 8 disulfide, 1 glycan (disulfide, N-glycosylation).
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 P14207
- Elsewhere: RCSB PDB 4KMY · PDBe 4KMY · UniProt P14207
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.