Research workbench
Crystal structure of human folate receptor alpha in complex with folic acid
Analyse Crystal structure of human folate receptor alpha in complex with folic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LRH
- Type
- protein
- Length
- 1,653 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Folate receptor alpha
- UniProt
- P15328
- Ligands
- FOL, NAG
- Pockets
- 18 · best druggability 0.75
Structure
x-ray diffraction · 8 distinct chains · 33% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Folate receptor alpha | protein | 207 | 33% helix, 11% strand | P15328 |
| B | Folate receptor alpha | protein | 204 | 34% helix, 10% strand | P15328 |
| C | Folate receptor alpha | protein | 209 | 34% helix, 10% strand | P15328 |
| D | Folate receptor alpha | protein | 210 | 32% helix, 10% strand | P15328 |
| E | Folate receptor alpha | protein | 206 | 33% helix, 11% strand | P15328 |
| F | Folate receptor alpha | protein | 208 | 32% helix, 11% strand | P15328 |
| G | Folate receptor alpha | protein | 205 | 31% helix, 11% strand | P15328 |
| H | Folate receptor alpha | protein | 204 | 32% helix, 11% strand | P15328 |
Ligands and binding sites
- FOL · Folic acid · ligand · 8 copies · chains A, B, C, D, E, F, G, H
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 22 copies · chains A, B, C, D, F, E, H, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 187 | 0.75 | 0.91 | 30 | FOL |
| 2 | 177 | 0.74 | 0.90 | 29 | FOL |
| 3 | 201 | 0.73 | 0.89 | 28 | FOL |
| 4 | 184 | 0.73 | 0.89 | 28 | FOL |
| 5 | 180 | 0.73 | 0.89 | 28 | FOL |
Interfaces
10 interfaces between chains.
- C–F · 700 Ų buried · 17 hydrogen bonds · protein-protein
- D–G · 664 Ų buried · 12 hydrogen bonds · protein-protein
- E–H · 657 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 648 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 230 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 64 disulfide, 22 glycan (disulfide, N-glycosylation).
Compared structures
- 4LRH · Crystal structure of human folate receptor alpha in complex with folic acid · the same entry in another collection · chain B against B, TM-score 1.00
- P15328 · AlphaFold monomer V2.0 prediction for folate receptor alpha (P15328) · a predicted model of the same protein · chain B 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 P15328
- Elsewhere: RCSB PDB 4LRH · PDBe 4LRH · UniProt P15328
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