MolNFT v1 · #18181 · protein
2:2 complex of G-csf with its receptor
1PGR · Protein (granulocyte colony-stimulating factor): “2:2 complex of G-csf with its receptor”. X-ray diffraction, 14 pockets (best druggability 0.62). MolNFT v1 #18181 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1PGR
- Type
- protein
- Length
- 1,471 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (granulocyte colony-stimulating factor); Protein (G-csf receptor)
- UniProt
- P09919, P40223
- Pockets
- 14 · best druggability 0.62
Structure
x-ray diffraction · 6 distinct chains · 34% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (granulocyte colony-stimulating factor) | protein | 161 | 69% helix, 1% strand | P09919 |
| B | Protein (G-csf receptor) | protein | 208 | 6% helix, 46% strand | P40223 |
| C, G | Protein (granulocyte colony-stimulating factor) | protein | 165 | 69% helix, 0% strand | P09919 |
| D, H | Protein (G-csf receptor) | protein | 200 | 6% helix, 46% strand | P40223 |
| E | Protein (granulocyte colony-stimulating factor) | protein | 163 | 68% helix, 1% strand | P09919 |
| F | Protein (G-csf receptor) | protein | 209 | 6% helix, 45% strand | P40223 |
Pockets
14 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 50 | 0.62 | 0.94 | 15 | empty |
| 2 | 56 | 0.61 | 0.92 | 19 | empty |
| 3 | 340 | 0.58 | 0.76 | 34 | empty |
| 4 | 260 | 0.55 | 0.77 | 33 | empty |
| 5 | 242 | 0.53 | 0.76 | 31 | empty |
Interfaces
8 interfaces between chains.
- E–F · 819 Ų buried · 11 hydrogen bonds · protein-protein
- G–H · 812 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 803 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 785 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 330 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 28 disulfide (disulfide).
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 P09919
- Every structure of UniProt P40223
- Elsewhere: RCSB PDB 1PGR · PDBe 1PGR · UniProt P09919 · UniProt P40223
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