MolNFT v1 · #63699 · protein
Independent saturation of three trprs subsites generates a partially- assembled state similar to those observed in molecular simulations
3FHJ: “Independent saturation of three trprs subsites generates a partially- assembled state similar to those…”. X-ray diffraction. MolNFT v1 #63699 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3FHJ
- Type
- protein
- Length
- 1,749 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P00953
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 300 | — | P00953 |
| D | — | protein | 287 | — | P00953 |
| B | — | protein | 292 | — | P00953 |
| C | — | protein | 280 | — | P00953 |
| E | — | protein | 293 | — | P00953 |
| F | — | protein | 297 | — | P00953 |
Compared structures
- 3FHJ · Independent saturation of three TrpRS subsites generates a partially-assembled state… · the same entry in another collection · chain A against A, TM-score 1.00
- P00953 · AlphaFold monomer V2.0 prediction for tryptophan--tRNA ligase (P00953) · a predicted model of the same protein · chain F against A, TM-score 0.97
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 P00953
- Elsewhere: RCSB PDB 3FHJ · PDBe 3FHJ · UniProt P00953
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