MolNFT v1 · #70322 · protein
Dfp modified degs delta PDZ
3LH3 · Protease degs: “Dfp modified degs delta PDZ”. X-ray diffraction, 15 pockets (best druggability 0.70). MolNFT v1 #70322 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3LH3
- Type
- protein
- Length
- 1,853 residues
- Chains
- 9
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protease degs
- EC
- 3.4.21.-
- UniProt
- P0AEE3
- Pockets
- 15 · best druggability 0.70
Structure
x-ray diffraction · 9 distinct chains · 15% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protease degs (EC 3.4.21.-) | protein | 207 | 14% helix, 41% strand | P0AEE3 |
| B | Protease degs (EC 3.4.21.-) | protein | 213 | 15% helix, 39% strand | P0AEE3 |
| C | Protease degs (EC 3.4.21.-) | protein | 214 | 14% helix, 39% strand | P0AEE3 |
| D | Protease degs (EC 3.4.21.-) | protein | 212 | 15% helix, 41% strand | P0AEE3 |
| E | Protease degs (EC 3.4.21.-) | protein | 203 | 15% helix, 42% strand | P0AEE3 |
| F | Protease degs (EC 3.4.21.-) | protein | 211 | 16% helix, 39% strand | P0AEE3 |
| G | Protease degs (EC 3.4.21.-) | protein | 202 | 16% helix, 37% strand | P0AEE3 |
| H | Protease degs (EC 3.4.21.-) | protein | 193 | 13% helix, 37% strand | P0AEE3 |
| I | Protease degs (EC 3.4.21.-) | protein | 198 | 15% helix, 40% strand | P0AEE3 |
Pockets
15 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 60 | 0.70 | 0.98 | 19 | empty |
| 2 | 58 | 0.69 | 0.97 | 20 | empty |
| 3 | 52 | 0.69 | 0.98 | 17 | empty |
| 4 | 794 | 0.68 | 0.75 | 63 | empty |
| 5 | 604 | 0.62 | 0.74 | 71 | empty |
Interfaces
15 interfaces between chains.
- A–B · 1373 Ų buried · 30 hydrogen bonds · protein-protein
- G–I · 1326 Ų buried · 29 hydrogen bonds · protein-protein
- E–F · 1310 Ų buried · 28 hydrogen bonds · protein-protein
- B–C · 1308 Ų buried · 25 hydrogen bonds · protein-protein
- G–H · 1276 Ų buried · 26 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 9 modified (nonstandard).
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 3LH3 · PDBe 3LH3 · UniProt P0AEE3
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