Research workbench
T6SS protein tssm C-terminal domain (869-1107) from eaec
Analyse T6SS protein tssm C-terminal domain (869-1107) from eaec in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4Y7L
- Type
- protein
- Length
- 474 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Type VI secretion protein icmf
- UniProt
- A0A070IVV8
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Type VI secretion protein icmf | protein | 235 | 31% helix, 30% strand | A0A070IVV8 |
| B | Type VI secretion protein icmf | protein | 239 | 30% helix, 31% strand | A0A070IVV8 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 229 | 0.57 | 0.79 | 38 | GOL |
| 2 | 315 | 0.56 | 0.76 | 41 | empty |
| 3 | 157 | 0.46 | 0.76 | 24 | ZN |
Interfaces
1 interface between chains.
- A–B · 840 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 4Y7L · T6SS protein TssM C-terminal domain (869-1107) from EAEC · the same entry in another collection · chain A against A, 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 A0A070IVV8
- Elsewhere: RCSB PDB 4Y7L · PDBe 4Y7L · UniProt A0A070IVV8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.