Research workbench
Ev-A71 strain 11316 complexed with tryptophan dendrimer MADAL_0385
Analyse Ev-A71 strain 11316 complexed with tryptophan dendrimer MADAL_0385 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DIZ
- Type
- protein
- Length
- 842 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- D4QGA8, I6W7A3, A0A0E3SXU7, M4QLY4
- Ligands
- SPH
Structure
electron microscopy · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 297 | — | D4QGA8 |
| B | — | protein | 245 | — | I6W7A3 |
| C | — | protein | 242 | — | A0A0E3SXU7 |
| D | — | protein | 58 | — | M4QLY4 |
Ligands and binding sites
- SPH · Sphingosine · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6DIZ · EV-A71 strain 11316 complexed with tryptophan dendrimer MADAL_0385 · 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 D4QGA8
- Every structure of UniProt I6W7A3
- Every structure of UniProt A0A0E3SXU7
- Every structure of UniProt M4QLY4
- Elsewhere: RCSB PDB 6DIZ · PDBe 6DIZ · UniProt D4QGA8 · UniProt I6W7A3 · UniProt A0A0E3SXU7 · UniProt M4QLY4
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