Research workbench
Phage display derived variant of human growth hormone complexed with two copies of the extracellular domain of its receptor
Analyse Phage display derived variant of human growth hormone complexed with two copies… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KF9
- Type
- protein
- Length
- 1,063 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phage display derived variant human growth hormone; Extracellular domain human growth…
- UniProt
- P10912
- Pockets
- 10 · best druggability 0.75
Structure
x-ray diffraction · 6 distinct chains · 21% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phage display derived variant human growth hormone | protein | 160 | 68% helix, 0% strand | — |
| B | Extracellular domain human growth hormone receptor (1-238) | protein | 193 | 2% helix, 48% strand | P10912 |
| C | Extracellular domain human growth hormone receptor (1-238) | protein | 175 | 0% helix, 46% strand | P10912 |
| D | Phage display derived variant human growth hormone | protein | 158 | 68% helix, 0% strand | — |
| E | Extracellular domain human growth hormone receptor (1-238) | protein | 193 | 2% helix, 48% strand | P10912 |
| F | Extracellular domain human growth hormone receptor (1-238) | protein | 184 | 0% helix, 49% strand | P10912 |
Pockets
10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1153 | 0.75 | 0.78 | 123 | empty |
| 2 | 597 | 0.64 | 0.75 | 69 | empty |
| 3 | 203 | 0.58 | 0.80 | 27 | empty |
| 4 | 187 | 0.58 | 0.81 | 26 | empty |
| 5 | 180 | 0.56 | 0.81 | 28 | empty |
Interfaces
9 interfaces between chains.
- A–B · 1171 Ų buried · 19 hydrogen bonds · protein-protein
- D–E · 1154 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 715 Ų buried · 11 hydrogen bonds · protein-protein
- D–F · 667 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 494 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 disulfide (disulfide).
Compared structures
- 1KF9 · Phage display derived variant of human growth hormone complexed with two copies of the… · the same entry in another collection · chain F against F, 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 0.97
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 P10912
- Elsewhere: RCSB PDB 1KF9 · PDBe 1KF9 · UniProt P10912
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