Research workbench
Crystal structure of human follicle stimulating hormone complexed with its receptor
Analyse Crystal structure of human follicle stimulating hormone complexed with its… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1XWD
- Type
- protein
- Length
- 862 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glycoprotein hormones alpha chain; Follitropin beta chain; Follicle stimulating hormone…
- UniProt
- P01215, P01225, P23945
- Ligands
- NAG, BMA, SO4
- Pockets
- 8 · best druggability 0.78
Structure
x-ray diffraction · 5 distinct chains · 1% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycoprotein hormones alpha chain | protein | 90 | 4% helix, 56% strand | P01215 |
| B, E | Follitropin beta chain | protein | 105 | 0% helix, 60% strand | P01225 |
| C | Follicle stimulating hormone receptor | protein | 242 | 0% helix, 28% strand | P23945 |
| D | Glycoprotein hormones alpha chain | protein | 87 | 3% helix, 52% strand | P01215 |
| F | Follicle stimulating hormone receptor | protein | 233 | 0% helix, 31% strand | P23945 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 10 copies · chains C, F, A, B, D, E
- BMA · beta-D-mannopyranose · sugar
- SO4 · Sulfate ion · ion · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 670 | 0.78 | 0.83 | 60 | empty |
| 2 | 740 | 0.78 | 0.82 | 68 | empty |
| 3 | 241 | 0.57 | 0.78 | 37 | empty |
| 4 | 214 | 0.56 | 0.79 | 24 | empty |
| 5 | 81 | 0.38 | 0.78 | 24 | empty |
Interfaces
7 interfaces between chains.
- A–B · 2272 Ų buried · 40 hydrogen bonds · protein-protein
- D–E · 2218 Ų buried · 36 hydrogen bonds · protein-protein
- D–F · 910 Ų buried · 18 hydrogen bonds · protein-protein
- A–C · 862 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 671 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 26 disulfide, 8 glycan (disulfide, N-glycosylation).
Compared structures
- 1XWD · Crystal Structure of Human Follicle Stimulating Hormone Complexed with its Receptor · the same entry in another collection · chain F against F, TM-score 1.00
- P23945 · AlphaFold monomer V2.0 prediction for follicle-stimulating hormone receptor (P23945) · a predicted model of the same protein · chain F against A, TM-score 0.99
- P01225 · AlphaFold monomer V2.0 prediction for follitropin subunit beta (P01225) · a predicted model of the same protein · chain B against A, TM-score 0.98
- P01215 · AlphaFold monomer V2.0 prediction for glycoprotein hormones alpha chain (P01215) · a predicted model of the same protein · chain D against A, TM-score 0.96
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 P01215
- Every structure of UniProt P01225
- Every structure of UniProt P23945
- Elsewhere: RCSB PDB 1XWD · PDBe 1XWD · UniProt P01215 · UniProt P01225 · UniProt P23945
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