Research workbench
D-tyr-TRNA(TYR) deacylase from plasmodium falciparum in complex with hepes
Analyse D-tyr-TRNA(TYR) deacylase from plasmodium falciparum in complex with hepes in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LMV
- Type
- protein
- Length
- 881 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q8IIS0
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 152 | — | Q8IIS0 |
| B | — | protein | 152 | — | Q8IIS0 |
| C | — | protein | 151 | — | Q8IIS0 |
| D | — | protein | 150 | — | Q8IIS0 |
| E | — | protein | 133 | — | Q8IIS0 |
| F | — | protein | 143 | — | Q8IIS0 |
Compared structures
- 3LMV · D-Tyr-tRNA(Tyr) Deacylase from plasmodium falciparum in complex with hepes · the same entry in another collection · chain C against C, TM-score 1.00
- Q8IIS0 · AlphaFold monomer V2.0 prediction for D-aminoacyl-tRNA deacylase (Q8IIS0) · a predicted model of the same protein · chain F against A, TM-score 0.99
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 Q8IIS0
- Elsewhere: RCSB PDB 3LMV · PDBe 3LMV · UniProt Q8IIS0
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