MolNFT v2 · #63701 · 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 at 2.65. MolNFT v2 #63701 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 v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.65
- Source
- Bacillus stearothermophilus
- UniProt
- P00953
Structure
x-ray diffraction · resolution 2.65 · 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
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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