Research workbench
Crystal structure of P97-N in complex with FAF1-ubx
Analyse Crystal structure of P97-N in complex with FAF1-ubx in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QQ8
- Type
- protein
- Length
- 257 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transitional endoplasmic reticulum ATPase; Fas-associated factor 1
- UniProt
- P55072, Q9UNN5
- Ligands
- CL
- Pockets
- 1 · best druggability 0.27
Structure
x-ray diffraction · 2 distinct chains · 17% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Transitional endoplasmic reticulum ATPase | protein | 177 | 17% helix, 38% strand | P55072 |
| B | Fas-associated factor 1 | protein | 80 | 16% helix, 41% strand | Q9UNN5 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 64 | 0.27 | 0.73 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 896 Ų buried · 9 hydrogen bonds · protein-protein
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 P55072
- Every structure of UniProt Q9UNN5
- Elsewhere: RCSB PDB 3QQ8 · PDBe 3QQ8 · UniProt P55072 · UniProt Q9UNN5
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