Research workbench
Engineered TTLL6 mutant bound to alpha-elongation analog
Analyse Engineered TTLL6 mutant bound to alpha-elongation analog in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VZQ
- Type
- protein
- Length
- 1,605 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A4Q9E8
- Ligands
- ADP, RZP, RZY, MG
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 400 | — | A4Q9E8 |
| B | — | protein | 398 | — | A4Q9E8 |
| C | — | protein | 403 | — | A4Q9E8 |
| D | — | protein | 404 | — | A4Q9E8 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 4 copies · chains A, B, C, D
- RZP · (2~{S})-2-[[[(1~{R})-1-acetamido-4-oxidanyl-4-oxidanylidene-butyl]-phosphonooxy-phosphoryl]methyl]pentanedioic acid · ligand · 3 copies · chains B, D, A, C
- RZY · (2~{S})-2-[[[(1~{S})-1-acetamidoethyl]-phosphonooxy-phosphoryl]methyl]pentanedioic acid · ligand · chains A
- MG · Magnesium ion · metal · 8 copies · chains A, B, C, D
- GOL · Glycerol · additive · 18 copies · chains B, D, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
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 A4Q9E8
- Elsewhere: RCSB PDB 6VZQ · PDBe 6VZQ · UniProt A4Q9E8
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