Research workbench
B.LICHENIFORMIS anti-trap can assemble into two types of dodecameric particles with the same symmetry but inverted orientation of trimers
Analyse B.LICHENIFORMIS anti-trap can assemble into two types of dodecameric particles… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LCZ
- Type
- protein
- Length
- 212 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inhibitor of trap, regulated by T-box (TRP) sequence rtpa
- UniProt
- Q65NU7
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.43
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Inhibitor of trap, regulated by T-box (TRP) sequence rtpa | protein | 53 | 32% helix, 19% strand | Q65NU7 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 53 | 0.43 | 0.83 | 16 | empty |
| 2 | 89 | 0.34 | 0.74 | 18 | empty |
Interfaces
5 interfaces between chains.
- A–C · 705 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 701 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 699 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 431 Ų buried · 1 hydrogen bond · protein-protein
- C–D · 97 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 3LCZ · B.licheniformis Anti-TRAP can assemble into two types of dodecameric particles with the… · 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 Q65NU7
- Elsewhere: RCSB PDB 3LCZ · PDBe 3LCZ · UniProt Q65NU7
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