Research workbench
Crystal structure of FAF1 ubx domain in complex with P97/VCP N domain reveals the conserved fcisp touch-turn motif of ubx domain suffering conformational change
Analyse Crystal structure of FAF1 ubx domain in complex with P97/VCP N domain reveals… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QCA
- Type
- protein
- Length
- 320 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fas-associated factor 1
- UniProt
- Q9UNN5
- Pockets
- 3 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Fas-associated factor 1 | protein | 80 | 20% helix, 39% strand | Q9UNN5 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 536 | 0.75 | 0.83 | 53 | empty |
| 2 | 292 | 0.56 | 0.76 | 29 | empty |
| 3 | 154 | 0.49 | 0.78 | 25 | empty |
Interfaces
6 interfaces between chains.
- A–C · 524 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 467 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 459 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 211 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 210 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3QCA · Crystal Structure of FAF1 UBX Domain In Complex with p97/VCP N Domain Reveals The… · the same entry in another collection · chain D against D, TM-score 1.00
- Q9UNN5 · AlphaFold monomer V2.0 prediction for fas-associated factor 1 (Q9UNN5) · a predicted model of the same protein · chain D 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 Q9UNN5
- Elsewhere: RCSB PDB 3QCA · PDBe 3QCA · UniProt Q9UNN5
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