Research workbench
Crystal structure of human chorionic gonadotropin
Analyse Crystal structure of human chorionic gonadotropin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HRP
- Type
- protein
- Length
- 196 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Human chorionic gonadotropin
- UniProt
- P01215, P01233
- Ligands
- NAG
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 2% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Human chorionic gonadotropin | protein | 86 | 5% helix, 59% strand | P01215 |
| B | Human chorionic gonadotropin | protein | 110 | 0% helix, 46% strand | P01233 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 204 | 0.57 | 0.79 | 33 | empty |
| 2 | 144 | 0.42 | 0.75 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 2056 Ų buried · 38 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 11 disulfide, 4 glycan (disulfide, N-glycosylation).
Compared structures
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 P01233
- Elsewhere: RCSB PDB 1HRP · PDBe 1HRP · UniProt P01215 · UniProt P01233
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