Research workbench
Human growth hormone bound to single receptor
Analyse Human growth hormone bound to single receptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1A22
- Type
- protein
- Length
- 372 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Growth hormone; Growth hormone receptor
- UniProt
- P01241, P10912
- Pockets
- 4 · best druggability 0.49
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Growth hormone | protein | 180 | 72% helix, 0% strand | P01241 |
| B | Growth hormone receptor | protein | 192 | 2% helix, 48% strand | P10912 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 146 | 0.49 | 0.78 | 27 | empty |
| 2 | 167 | 0.47 | 0.76 | 27 | empty |
| 3 | 84 | 0.38 | 0.77 | 17 | empty |
| 4 | 73 | 0.36 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1391 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 1A22 · Human growth hormone bound to single receptor · the same entry in another collection · chain A against A, TM-score 1.00
- P10912 · AlphaFold monomer V2.0 prediction for growth hormone receptor (P10912) · a predicted model of the same protein · chain B against A, TM-score 0.98
- P01241 · AlphaFold monomer V2.0 prediction for somatotropin (P01241) · a predicted model of the same protein · chain A against A, TM-score 0.86
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 P01241
- Every structure of UniProt P10912
- Elsewhere: RCSB PDB 1A22 · PDBe 1A22 · UniProt P01241 · UniProt P10912
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