Research workbench
Enterococcus italicus CSM6 bound to cyclic hexa-2'-fluoro-hexa-damp
Analyse Enterococcus italicus CSM6 bound to cyclic hexa-2'-fluoro-hexa-damp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TUG
- Type
- protein
- Length
- 3,282 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- E6LHV2
- Ligands
- AF2, SO4
Structure
x-ray diffraction · 7 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | — | protein | 408 | — | E6LHV2 |
| B | — | protein | 415 | — | E6LHV2 |
| D | — | protein | 406 | — | E6LHV2 |
| E | — | protein | 409 | — | E6LHV2 |
| F | — | protein | 415 | — | E6LHV2 |
| G | — | protein | 407 | — | E6LHV2 |
| H | — | protein | 414 | — | E6LHV2 |
Ligands and binding sites
- AF2 · 2'-deoxy-2'-fluoroadenosine 5'-(dihydrogen phosphate) · ligand · 24 copies · chains A, B, C, D, E, F, G, H
- SO4 · Sulfate ion · ion · 4 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6TUG · Enterococcus italicus Csm6 bound to cyclic hexa-2'-fluoro-hexa-dAMP · the same entry in another collection · chain H against H, TM-score 1.00
- E6LHV2 · AlphaFold monomer V2.0 prediction for CRISPR system endoribonuclease CSM6 (E6LHV2) · a predicted model of the same protein · chain H against A, TM-score 0.72
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 E6LHV2
- Elsewhere: RCSB PDB 6TUG · PDBe 6TUG · UniProt E6LHV2
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.