Research workbench
Structural dynamics of the meca-clpc complex revealed by cryo-EM
Analyse Structural dynamics of the meca-clpc complex revealed by cryo-EM in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3J3U
- Type
- protein
- Length
- 5,352 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adapter protein meca 1; Negative regulator of genetic competence CLPC/MECB
- UniProt
- P37958, P37571
- Pockets
- 20 · best druggability 0.80
Structure
electron microscopy · 2 distinct chains · 49% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 1, 2, 3, 4, 5, 6 | Adapter protein meca 1 | protein | 94 | 40% helix, 30% strand | P37958 |
| A, B, C, D, E, F | Negative regulator of genetic competence CLPC/MECB | protein | 798 | 50% helix, 9% strand | P37571 |
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 | 966 | 0.80 | 0.82 | 74 | empty |
| 2 | 966 | 0.80 | 0.82 | 67 | empty |
| 3 | 694 | 0.79 | 0.84 | 63 | empty |
| 4 | 857 | 0.78 | 0.81 | 67 | empty |
| 5 | 737 | 0.77 | 0.82 | 65 | empty |
Interfaces
22 interfaces between chains.
- D–E · 3679 Ų buried · 114 hydrogen bonds · protein-protein
- A–B · 3615 Ų buried · 102 hydrogen bonds · protein-protein
- B–C · 3572 Ų buried · 89 hydrogen bonds · protein-protein
- E–F · 3569 Ų buried · 89 hydrogen bonds · protein-protein
- A–F · 3511 Ų buried · 102 hydrogen bonds · protein-protein
Compared structures
- 3J3U · Structural dynamics of the MecA-ClpC complex revealed by cryo-EM · the same entry in another collection · chain F against F, 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 P37958
- Every structure of UniProt P37571
- Elsewhere: RCSB PDB 3J3U · PDBe 3J3U · UniProt P37958 · UniProt P37571
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