Research workbench
Crystal structure of neisseria meningitidis clpp E58A activated mutant
Analyse Crystal structure of neisseria meningitidis clpp E58A activated mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NAW
- Type
- protein
- Length
- 2,498 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
- I4E574
- Pockets
- 20 · best druggability 0.73
Structure
x-ray diffraction · 12 distinct chains · 47% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 177 | 47% helix, 23% strand | I4E574 |
| B | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 178 | 47% helix, 22% strand | I4E574 |
| C, L | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 175 | 47% helix, 23% strand | I4E574 |
| D, F | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 179 | 46% helix, 23% strand | I4E574 |
| E | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 177 | 47% helix, 23% strand | I4E574 |
| G | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 183 | 46% helix, 23% strand | I4E574 |
| H | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 180 | 46% helix, 22% strand | I4E574 |
| I | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 178 | 47% helix, 22% strand | I4E574 |
| J | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 180 | 47% helix, 22% strand | I4E574 |
| K | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 183 | 45% helix, 22% strand | I4E574 |
| M | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 178 | 47% helix, 24% strand | I4E574 |
| N | ATP-dependent clp protease proteolytic subunit (EC 3.4.21.92) | protein | 176 | 47% helix, 22% strand | I4E574 |
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 419 | 0.73 | 0.83 | 70 | empty |
| 2 | 741 | 0.72 | 0.78 | 101 | empty |
| 3 | 451 | 0.72 | 0.81 | 81 | empty |
| 4 | 337 | 0.70 | 0.82 | 65 | empty |
| 5 | 405 | 0.67 | 0.79 | 69 | empty |
Interfaces
35 interfaces between chains.
- H–N · 1516 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 1511 Ų buried · 20 hydrogen bonds · protein-protein
- A–G · 1509 Ų buried · 18 hydrogen bonds · protein-protein
- L–M · 1506 Ų buried · 20 hydrogen bonds · protein-protein
- F–G · 1501 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 6NAW · Crystal structure of Neisseria meningitidis ClpP E58A activated mutant · the same entry in another collection · chain N against N, 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 I4E574
- Elsewhere: RCSB PDB 6NAW · PDBe 6NAW · UniProt I4E574
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