Research workbench
Solution structure of the a-subunit of human chorionic gonadotropin [modeled with diantennary glycan at ASN78]
Analyse Solution structure of the a-subunit of human chorionic gonadotropin [modeled… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HD4
- Type
- protein
- Length
- 92 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chorionic gonadotropin
- UniProt
- P01215
- Ligands
- NAG, MAN, GAL, BMA
- Pockets
- 1 · best druggability 0.33
Structure
solution nmr · 1 distinct chain · 0% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chorionic gonadotropin | protein | 92 | 0% helix, 9% strand | P01215 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
- MAN · alpha-D-mannopyranose · sugar · 2 copies
- GAL · beta-D-galactopyranose · sugar · 2 copies
- BMA · beta-D-mannopyranose · sugar
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 104 | 0.33 | 0.72 | 24 | empty |
Modifications
Observed in the structure: 5 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 1HD4 · Solution structure of the a-subunit of human chorionic gonadotropin [modeled with… · the same entry in another collection · chain A against A, TM-score 1.00
- 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 0.50
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
- Elsewhere: RCSB PDB 1HD4 · PDBe 1HD4 · UniProt P01215
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