Research workbench
Structural model of parm filament in the open state by cryo- EM
Analyse Structural model of parm filament in the open state 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
- 3IKY
- Type
- protein
- Length
- 3,840 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Plasmid segregation protein parm
- UniProt
- P11904
- Pockets
- 20 · best druggability 0.72
Structure
electron microscopy · 1 distinct chain · 39% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | Plasmid segregation protein parm | protein | 320 | 39% helix, 24% strand | P11904 |
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 | 747 | 0.72 | 0.79 | 79 | empty |
| 2 | 778 | 0.72 | 0.78 | 83 | empty |
| 3 | 610 | 0.71 | 0.79 | 60 | empty |
| 4 | 623 | 0.71 | 0.79 | 56 | empty |
| 5 | 661 | 0.71 | 0.78 | 65 | empty |
Interfaces
21 interfaces between chains.
- A–C · 795 Ų buried · 21 hydrogen bonds · protein-protein
- C–E · 794 Ų buried · 21 hydrogen bonds · protein-protein
- D–F · 793 Ų buried · 21 hydrogen bonds · protein-protein
- J–L · 792 Ų buried · 21 hydrogen bonds · protein-protein
- F–H · 792 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 isopeptide (isopeptide).
Compared structures
- 3IKY · Structural model of ParM filament in the open state by cryo-EM · the same entry in another collection · chain L against L, 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 P11904
- Elsewhere: RCSB PDB 3IKY · PDBe 3IKY · UniProt P11904
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