MolNFT v1 · #33866 · protein
Crystal structure of an N-terminal fragment of the phenylalanyl-tRNA synthetase beta-subunit from pyrococcus horikoshii
2CXI · Phenylalanyl-tRNA synthetase beta chain: “Crystal structure of an N-terminal fragment of the phenylalanyl-tRNA synthetase beta-subunit from pyrococcus…”. X-ray diffraction, 8 pockets (best druggability 0.64). MolNFT v1 #33866 on…
- PDB
- 2CXI
- Type
- protein
- Length
- 1,041 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phenylalanyl-tRNA synthetase beta chain
- EC
- 6.1.1.20
- UniProt
- O73984
- Pockets
- 8 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Phenylalanyl-tRNA synthetase beta chain (EC 6.1.1.20) | protein | 347 | 34% helix, 31% strand | O73984 |
Pockets
8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 237 | 0.64 | 0.82 | 28 | empty |
| 2 | 480 | 0.63 | 0.76 | 46 | empty |
| 3 | 238 | 0.63 | 0.82 | 32 | empty |
| 4 | 201 | 0.62 | 0.82 | 27 | empty |
| 5 | 476 | 0.58 | 0.74 | 42 | empty |
Interfaces
2 interfaces between chains.
- B–C · 934 Ų buried · 19 hydrogen bonds · protein-protein
- A–C · 495 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 modified (engineered).
Compared structures
- 2CXI · Crystal Structure Of An N-terminal Fragment Of The Phenylalanyl-tRNA Synthetase… · the same entry in another collection · chain A against A, TM-score 1.00
- O73984 · AlphaFold monomer V2.0 prediction for phenylalanine--tRNA ligase beta subunit (O73984) · a predicted model of the same protein · chain A 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 O73984
- Elsewhere: RCSB PDB 2CXI · PDBe 2CXI · UniProt O73984
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