Research workbench
Human follicle stimulating hormone
Analyse Human follicle stimulating hormone in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FL7
- Type
- protein
- Length
- 387 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Follicle stimulating protein alpha chain; Follicle stimulating protein beta chain
- UniProt
- P01215, P01225
- Ligands
- NAG, NDG, MAN, SO4
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 4 distinct chains · 5% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Follicle stimulating protein alpha chain | protein | 86 | 7% helix, 49% strand | P01215 |
| B | Follicle stimulating protein beta chain | protein | 107 | 3% helix, 50% strand | P01225 |
| C | Follicle stimulating protein alpha chain | protein | 88 | 9% helix, 53% strand | P01215 |
| D | Follicle stimulating protein beta chain | protein | 106 | 3% helix, 58% strand | P01225 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 9 copies · chains A, B, C, D
- NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar · 3 copies · chains D, C
- MAN · alpha-D-mannopyranose · sugar · 2 copies
- SO4 · Sulfate ion · ion · 2 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 853 | 0.74 | 0.78 | 96 | SO4 |
| 2 | 64 | 0.47 | 0.83 | 22 | empty |
| 3 | 118 | 0.47 | 0.79 | 27 | empty |
| 4 | 127 | 0.44 | 0.77 | 30 | SO4 |
| 5 | 73 | 0.32 | 0.74 | 14 | empty |
Interfaces
6 interfaces between chains.
- A–B · 2116 Ų buried · 40 hydrogen bonds · protein-protein
- C–D · 1950 Ų buried · 35 hydrogen bonds · protein-protein
- A–D · 465 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 325 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 276 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 22 disulfide, 6 glycan (disulfide, N-glycosylation).
Compared structures
- 1FL7 · Human follicle stimulating hormone · the same entry in another collection · chain D against D, TM-score 1.00
- P01225 · AlphaFold monomer V2.0 prediction for follitropin subunit beta (P01225) · a predicted model of the same protein · chain D against A, TM-score 0.93
- P01215 · AlphaFold monomer V2.0 prediction for glycoprotein hormones alpha chain (P01215) · a predicted model of the same protein · chain A against A, TM-score 0.91
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
- Elsewhere: RCSB PDB 1FL7 · PDBe 1FL7 · UniProt P01215 · UniProt P01225
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