Research workbench
Human folate receptor beta (FOLR2) in complex with the antifolate methotrexate
Analyse Human folate receptor beta (FOLR2) in complex with the antifolate methotrexate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KN0
- Type
- protein
- Length
- 205 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Folate receptor beta
- UniProt
- P14207
- Ligands
- MTX, NAG, K, CL
- Pockets
- 1 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Folate receptor beta | protein | 205 | 32% helix, 10% strand | P14207 |
Ligands and binding sites
- MTX · Methotrexate · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
- K · Potassium ion · metal · chains A
- CL · Chloride ion · ion · 2 copies · 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 | 236 | 0.77 | 0.90 | 28 | MTX |
Modifications
Observed in the structure: 8 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
- 4KN0 · Human folate receptor beta (FOLR2) in complex with the antifolate methotrexate · the same entry in another collection · chain A against A, TM-score 1.00
- P14207 · AlphaFold monomer V2.0 prediction for folate receptor beta (P14207) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 4KN0 · PDBe 4KN0 · UniProt P14207
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