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Crystal structure of hausp
Analyse Crystal structure of hausp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2F1Z
- Type
- protein
- Length
- 951 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquitin carboxyl-terminal hydrolase 7
- EC
- 3.1.2.15
- UniProt
- Q93009
- Pockets
- 12 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 21% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ubiquitin carboxyl-terminal hydrolase 7 (EC 3.1.2.15) | protein | 470 | 21% helix, 31% strand | Q93009 |
| B | Ubiquitin carboxyl-terminal hydrolase 7 (EC 3.1.2.15) | protein | 481 | 21% helix, 29% strand | Q93009 |
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1048 | 0.85 | 0.85 | 91 | empty |
| 2 | 212 | 0.62 | 0.82 | 32 | empty |
| 3 | 251 | 0.57 | 0.78 | 32 | empty |
| 4 | 324 | 0.57 | 0.76 | 36 | empty |
| 5 | 73 | 0.47 | 0.83 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1837 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 2F1Z · Crystal structure of HAUSP · the same entry in another collection · chain A against A, 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
- Every structure of UniProt Q93009
- Elsewhere: RCSB PDB 2F1Z · PDBe 2F1Z · UniProt Q93009
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