MolNFT v1 · #4515 · protein
Crystal structure of Fab hgr-2 F6, a competitive antagonist of the glucagon receptor
1DQD: “Crystal structure of Fab hgr-2 F6, a competitive antagonist of the glucagon receptor”. X-ray diffraction, 6 pockets (best druggability 0.51). MolNFT v1 #4515 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1DQD
- Type
- protein
- Length
- 435 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fab hgr-2 F6
- Pockets
- 6 · best druggability 0.51
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | Fab hgr-2 F6 | protein | 214 | 5% helix, 50% strand | — |
| H | Fab hgr-2 F6 | protein | 221 | 5% helix, 52% strand | — |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 264 | 0.51 | 0.75 | 37 | empty |
| 2 | 132 | 0.46 | 0.78 | 23 | empty |
| 3 | 169 | 0.45 | 0.75 | 28 | empty |
| 4 | 98 | 0.41 | 0.77 | 16 | empty |
| 5 | 79 | 0.33 | 0.74 | 22 | empty |
Interfaces
1 interface between chains.
- L–H · 1928 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1DQD · Crystal structure of Fab hgr-2 F6, a competitive antagonist of the glucagon receptor · the same entry in another collection · chain L against L, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 1DQD · PDBe 1DQD
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