MolNFT v1 · #81869 · protein
Crystal structure of clpp from staphylococcus aureus in the active, extended conformation
3V5E · ATP-dependent clp protease proteolytic subunit: “Crystal structure of clpp from staphylococcus aureus in the active, extended conformation”. X-ray diffraction, 20 pockets (best druggability 0.64). MolNFT v1 #81869 on GenesisL1: 3D…
- PDB
- 3V5E
- Type
- protein
- Length
- 2,576 residues
- Chains
- 14
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent clp protease proteolytic subunit
- EC
- 3.4.21.92
- UniProt
- Q2G036
- Pockets
- 20 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 45% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 184 | 45% helix, 26% strand | Q2G036 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 336 | 0.64 | 0.79 | 54 | empty |
| 2 | 338 | 0.63 | 0.79 | 60 | empty |
| 3 | 344 | 0.61 | 0.78 | 51 | empty |
| 4 | 285 | 0.61 | 0.79 | 51 | empty |
| 5 | 325 | 0.61 | 0.78 | 55 | empty |
Interfaces
35 interfaces between chains.
- M–N · 1656 Ų buried · 12 hydrogen bonds · protein-protein
- H–N · 1653 Ų buried · 15 hydrogen bonds · protein-protein
- D–E · 1652 Ų buried · 14 hydrogen bonds · protein-protein
- J–K · 1645 Ų buried · 14 hydrogen bonds · protein-protein
- K–L · 1644 Ų buried · 15 hydrogen bonds · protein-protein
Compared structures
- 3V5E · Crystal structure of ClpP from Staphylococcus aureus in the active, extended conformation · the same entry in another collection · chain K against K, 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 Q2G036
- Elsewhere: RCSB PDB 3V5E · PDBe 3V5E · UniProt Q2G036
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