Research workbench
The structure of the FEM1B:FNIP1 complex
Analyse The structure of the FEM1B:FNIP1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ROY
- Type
- protein
- Length
- 1,543 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein fem-1 homolog B; Folliculin-interacting protein 1
- UniProt
- Q9Z2G0, Q68FD7
- Ligands
- ZN
- Pockets
- 18 · best druggability 0.83
Structure
x-ray diffraction · 6 distinct chains · 55% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein fem-1 homolog B | protein | 377 | 55% helix, 5% strand | Q9Z2G0 |
| B | Protein fem-1 homolog B | protein | 375 | 54% helix, 5% strand | Q9Z2G0 |
| C | Protein fem-1 homolog B | protein | 379 | 58% helix, 5% strand | Q9Z2G0 |
| D | Protein fem-1 homolog B | protein | 374 | 57% helix, 4% strand | Q9Z2G0 |
| G | Folliculin-interacting protein 1 | protein | 15 | 0% helix, 0% strand | Q68FD7 |
| H | Folliculin-interacting protein 1 | protein | 23 | 0% helix, 0% strand | Q68FD7 |
Ligands and binding sites
- ZN · Zinc ion · metal · 8 copies · chains A, G, B, C, H, D
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 4 copies · chains A, G, B, C, H, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 835 | 0.83 | 0.85 | 77 | EPE |
| 2 | 905 | 0.82 | 0.84 | 78 | EPE |
| 3 | 747 | 0.71 | 0.77 | 61 | empty |
| 4 | 261 | 0.69 | 0.85 | 37 | empty |
| 5 | 266 | 0.68 | 0.84 | 33 | empty |
Interfaces
7 interfaces between chains.
- B–C · 1397 Ų buried · 14 hydrogen bonds · protein-protein
- A–D · 1339 Ų buried · 13 hydrogen bonds · protein-protein
- C–H · 1004 Ų buried · 16 hydrogen bonds · protein-protein
- A–G · 756 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 437 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 7ROY · The structure of the Fem1B:FNIP1 complex · the same entry in another collection · chain H against H, TM-score 1.00
- Q9Z2G0 · AlphaFold monomer V2.0 prediction for protein fem-1 homolog B (Q9Z2G0) · a predicted model of the same protein · chain C against A, TM-score 0.98
- Q68FD7 · AlphaFold monomer V2.0 prediction for folliculin-interacting protein 1 (Q68FD7) · a predicted model of the same protein · chain G against A, TM-score 0.28
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 Q9Z2G0
- Every structure of UniProt Q68FD7
- Elsewhere: RCSB PDB 7ROY · PDBe 7ROY · UniProt Q9Z2G0 · UniProt Q68FD7
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