Research workbench
Structural model of parm filament in closed state from cryo- EM
Analyse Structural model of parm filament in closed state from cryo- EM in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3IKU
- Type
- protein
- Length
- 3,792 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 0.84
Structure
electron microscopy · 1 distinct chain · 38% helix, 23% 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 | 316 | 38% helix, 23% 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 | 963 | 0.84 | 0.85 | 109 | empty |
| 2 | 869 | 0.83 | 0.85 | 101 | empty |
| 3 | 795 | 0.83 | 0.86 | 94 | empty |
| 4 | 841 | 0.83 | 0.85 | 100 | empty |
| 5 | 767 | 0.82 | 0.86 | 87 | empty |
Interfaces
21 interfaces between chains.
- H–J · 805 Ų buried · 47 hydrogen bonds · protein-protein
- J–L · 801 Ų buried · 47 hydrogen bonds · protein-protein
- E–G · 798 Ų buried · 47 hydrogen bonds · protein-protein
- G–I · 797 Ų buried · 47 hydrogen bonds · protein-protein
- I–K · 796 Ų buried · 47 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 isopeptide (isopeptide).
Compared structures
- 3IKU · Structural model of ParM filament in closed state from 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 3IKU · PDBe 3IKU · UniProt P11904
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