MolNFT v1 · #50422 · protein
Phers from staphylococcus haemolyticus- rational protein engineering and inhibitor studies
2RHS: “Phers from staphylococcus haemolyticus- rational protein engineering and inhibitor studies”. X-ray diffraction. MolNFT v1 #50422 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2RHS
- Type
- protein
- Length
- 2,091 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q4L5E3, Q4L5E4
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 249 | — | Q4L5E3 |
| B | — | protein | 786 | — | Q4L5E4 |
| C | — | protein | 271 | — | Q4L5E3 |
| D | — | protein | 785 | — | Q4L5E4 |
Compared structures
- 2RHS · PheRS from Staphylococcus haemolyticus- rational protein engineering and inhibitor studies · the same entry in another collection · chain D against D, TM-score 1.00
- Q4L5E4 · AlphaFold monomer V2.0 prediction for phenylalanine--tRNA ligase beta subunit (Q4L5E4) · a predicted model of the same protein · chain D against A, TM-score 0.97
- Q4L5E3 · AlphaFold monomer V2.0 prediction for phenylalanine--tRNA ligase alpha subunit (Q4L5E3) · a predicted model of the same protein · chain A 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 Q4L5E3
- Every structure of UniProt Q4L5E4
- Elsewhere: RCSB PDB 2RHS · PDBe 2RHS · UniProt Q4L5E3 · UniProt Q4L5E4
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