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Crystal structure of the PDZ deletion mutant of degs
Analyse Crystal structure of the PDZ deletion mutant of degs in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2R3U
- Type
- protein
- Length
- 582 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protease degs
- EC
- 3.4.21.-
- UniProt
- P0AEE3
- Pockets
- 3 · best druggability 0.55
Structure
x-ray diffraction · 3 distinct chains · 14% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protease degs (EC 3.4.21.-) | protein | 202 | 12% helix, 43% strand | P0AEE3 |
| B | Protease degs (EC 3.4.21.-) | protein | 195 | 15% helix, 36% strand | P0AEE3 |
| C | Protease degs (EC 3.4.21.-) | protein | 185 | 16% helix, 39% strand | P0AEE3 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 225 | 0.55 | 0.78 | 46 | empty |
| 2 | 177 | 0.45 | 0.75 | 32 | empty |
| 3 | 62 | 0.32 | 0.75 | 12 | empty |
Interfaces
3 interfaces between chains.
- B–C · 1072 Ų buried · 21 hydrogen bonds · protein-protein
- A–B · 1061 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 1044 Ų buried · 14 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 P0AEE3
- Elsewhere: RCSB PDB 2R3U · PDBe 2R3U · UniProt P0AEE3
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