MolNFT v1 · #100434 · protein
Clpp SER98DHA
4MXI · ATP-dependent clp protease proteolytic subunit: “Clpp SER98DHA”. X-ray diffraction, 20 pockets (best druggability 0.49). MolNFT v1 #100434 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4MXI
- Type
- protein
- Length
- 1,184 residues
- Chains
- 7
- 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 0.49
Structure
x-ray diffraction · 6 distinct chains · 48% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 171 | 46% helix, 20% strand | Q2G036 |
| B | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 166 | 48% helix, 19% strand | Q2G036 |
| C | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 169 | 47% helix, 20% strand | Q2G036 |
| D | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 167 | 48% helix, 20% strand | Q2G036 |
| E, F | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 170 | 48% helix, 19% strand | Q2G036 |
| G | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 171 | 47% helix, 19% strand | Q2G036 |
Pockets
20 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 160 | 0.49 | 0.78 | 27 | empty |
| 2 | 168 | 0.49 | 0.77 | 26 | empty |
| 3 | 139 | 0.48 | 0.78 | 23 | empty |
| 4 | 121 | 0.45 | 0.77 | 28 | empty |
| 5 | 116 | 0.44 | 0.77 | 21 | empty |
Interfaces
7 interfaces between chains.
- A–B · 1413 Ų buried · 11 hydrogen bonds · protein-protein
- A–G · 1333 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 1309 Ų buried · 9 hydrogen bonds · protein-protein
- D–E · 1300 Ų buried · 7 hydrogen bonds · protein-protein
- F–G · 1286 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 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 Q2G036
- Elsewhere: RCSB PDB 4MXI · PDBe 4MXI · UniProt Q2G036
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