Research workbench
1:1 complex of human growth hormone mutant G120R with its soluble binding protein
Analyse 1:1 complex of human growth hormone mutant G120R with its soluble binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HWH
- Type
- protein
- Length
- 381 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Growth hormone; Growth hormone binding protein
- UniProt
- P01241, P10912
- Pockets
- 3 · best druggability 0.47
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Growth hormone | protein | 185 | 65% helix, 0% strand | P01241 |
| B | Growth hormone binding protein | protein | 196 | 4% helix, 44% strand | P10912 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 138 | 0.47 | 0.78 | 34 | empty |
| 2 | 78 | 0.39 | 0.78 | 18 | empty |
| 3 | 87 | 0.38 | 0.77 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 1352 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 1HWH · 1:1 complex of human growth hormone mutant G120R with its soluble binding protein · 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 0.85
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 1HWH · PDBe 1HWH · UniProt P01241 · UniProt P10912
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