MolNFT v1 · #158946 · protein
Ternary complex of mouse ecd with FAB1 and FAB2
6O9I · FAB1 heavy chain: “Ternary complex of mouse ecd with FAB1 and FAB2”. X-ray diffraction, 14 pockets (best druggability 0.74). MolNFT v1 #158946 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6O9I
- Type
- protein
- Length
- 950 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FAB1 heavy chain; FAB1 light chain; Gastric inhibitory polypeptide receptor; Fab 2 heavy…
- UniProt
- Q0P543
- Pockets
- 14 · best druggability 0.74
Structure
x-ray diffraction · 5 distinct chains · 8% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FAB1 heavy chain | protein | 217 | 6% helix, 53% strand | — |
| B | FAB1 light chain | protein | 217 | 6% helix, 53% strand | — |
| C | Gastric inhibitory polypeptide receptor | protein | 106 | 29% helix, 25% strand | Q0P543 |
| D | Fab 2 heavy chain | protein | 208 | 4% helix, 51% strand | — |
| E | FAB2 light chain | protein | 202 | 3% helix, 48% strand | — |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 5 copies · chains A, B, C, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 357 | 0.74 | 0.85 | 40 | empty |
| 2 | 712 | 0.66 | 0.75 | 66 | empty |
| 3 | 504 | 0.63 | 0.76 | 59 | empty |
| 4 | 158 | 0.51 | 0.79 | 28 | empty |
| 5 | 148 | 0.48 | 0.77 | 19 | EDO |
Interfaces
6 interfaces between chains.
- A–B · 1884 Ų buried · 15 hydrogen bonds · protein-protein
- D–E · 1781 Ų buried · 20 hydrogen bonds · protein-protein
- C–D · 545 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 532 Ų buried · 12 hydrogen bonds · protein-protein
- C–E · 357 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 11 disulfide, 1 modified (disulfide, cyclization).
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 Q0P543
- Elsewhere: RCSB PDB 6O9I · PDBe 6O9I · UniProt Q0P543
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