UniProt P0A0L5
P0A0L5
P0A0L5 (UniProt P0A0L5): 36 experimental structures and 1 predicted model on GenesisL1. Binding sites, druggability and experiment against prediction (TM-score) in GL1X.
- UniProt
- P0A0L5
- Experimental structures
- 36
- Predicted models
- 1
Structures
37 records of P0A0L5 in the MolNFT archive: 36 experimental, 1 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 1JCK | T-cell receptor beta chain complexed with SEC3 superantigen | x-ray diffraction | B, D | — | — |
| 1JCK | T-cell receptor beta chain complexed with SEC3 superantigen | x-ray diffraction | B, D | — | — |
| 1JWM | Crystal Structure of the Complex of the MHC Class II Molecule HLA-DR1(HA peptide 306-318) with the… | x-ray diffraction | D | — | — |
| 1JWM | Crystal structure of the complex of the MHC class II molecule HLA-DR1(HA peptide 306-318) with the… | x-ray diffraction | D | — | — |
| 1JWS | Crystal Structure of the Complex of the MHC Class II Molecule HLA-DR1 (HA peptide 306-318) with the… | x-ray diffraction | D | — | — |
| 1JWS | Crystal structure of the complex of the MHC class II molecule HLA-DR1 (ha peptide 306-318) with the… | x-ray diffraction | D | — | — |
| 1JWU | Crystal Structure of the Complex of the MHC Class II Molecule HLA-DR1 (HA peptide 306-318) with the… | x-ray diffraction | D | — | — |
| 1JWU | Crystal structure of the complex of the MHC class II molecule HLA-DR1 (ha peptide 306-318) with the… | x-ray diffraction | D | — | — |
| 1KLG | Crystal structure of HLA-DR1/TPI(23-37, Thr28-->Ile mutant) complexed with staphylococcal… | x-ray diffraction | D | — | — |
| 1KLG | Crystal structure of HLA-DR1/TPI(23-37, THR28-->ile mutant) complexed with staphylococcal… | x-ray diffraction | D | — | — |
| 1KLU | Crystal structure of HLA-DR1/TPI(23-37) complexed with staphylococcal enterotoxin C3 variant 3B2… | x-ray diffraction | D | — | — |
| 1KLU | Crystal structure of HLA-DR1/TPI(23-37) complexed with staphylococcal enterotoxin C3 variant 3B2… | x-ray diffraction | D | — | — |
| 1SJE | HLA-DR1 complexed with a 16 residue HIV capsid peptide bound in a hairpin conformation | x-ray diffraction | D | — | — |
| 1SJE | HLA-DR1 complexed with a 16 residue HIV capsid peptide bound in a hairpin conformation | x-ray diffraction | D | — | — |
| 1SJH | HLA-DR1 complexed with a 13 residue HIV capsid peptide | x-ray diffraction | D | — | — |
| 1SJH | HLA-DR1 complexed with a 13 residue HIV capsid peptide | x-ray diffraction | D | — | — |
| 1T5X | HLA-DR1 in complex with a synthetic peptide (AAYSDQATPLLLSPR) and the superantigen SEC3-3B2 | x-ray diffraction | D | — | — |
| 1T5X | HLA-DR1 in complex with a synthetic peptide (aaysdqatplllspr) and the superantigen SEC3-3B2 | x-ray diffraction | D | — | — |
| 2AQ1 | Crystal structure of T-cell receptor V beta domain variant complexed with superantigen SEC3 mutant | x-ray diffraction | B, D, F, H | — | — |
| 2AQ1 | Crystal structure of T-cell receptor V beta domain variant complexed with superantigen SEC3 mutant | x-ray diffraction | B, D, F, H | — | — |
| 2AQ2 | Crystal structure of T-cell receptor V beta domain variant complexed with superantigen SEC3 mutant | x-ray diffraction | B | — | — |
| 2AQ2 | Crystal structure of T-cell receptor V beta domain variant complexed with superantigen SEC3 mutant | x-ray diffraction | B | — | — |
| 2AQ3 | Crystal structure of T-cell receptor V beta domain variant complexed with superantigen SEC3 | x-ray diffraction | B, D, F, H | — | — |
| 2AQ3 | Crystal structure of T-cell receptor V beta domain variant complexed with superantigen SEC3 | x-ray diffraction | B, D, F, H | — | — |
| 3BVG | Manipulating the coupled folding and binding process drives affinity maturation in a… | x-ray diffraction | A | — | — |
| 3BVG | Manipulating the coupled folding and binding process drives affinity maturation in a… | x-ray diffraction | A | — | — |
| 3BVM | Manipulating the coupled folding and binding process drives affinity maturation in a… | x-ray diffraction | A | — | — |
| 3BVM | Manipulating the coupled folding and binding process drives affinity maturation in a… | x-ray diffraction | A | — | — |
| 3BVZ | Manipulating the coupled folding and binding process drives affinity maturation in a… | x-ray diffraction | A | — | — |
| 3BVZ | Manipulating the coupled folding and binding process drives affinity maturation in a… | x-ray diffraction | A | — | — |
| 3BYT | A complex between a variant of staphylococcal enterotoxin C3 and the variable domain of the murine… | x-ray diffraction | B, D, F, H | — | — |
| 3BYT | A complex between a variant of staphylococcal enterotoxin C3 and the variable domain of the murine… | x-ray diffraction | B, D, F, H | — | — |
| 3BYY | Manipulating the coupled folding and binding process drives affinity maturation in a… | x-ray diffraction | B | — | — |
| 3BYY | Manipulating the coupled folding and binding process drives affinity maturation in a… | x-ray diffraction | B | — | — |
| 3BZD | Manipulating the coupled folding and binding process drives affinity maturation in a… | x-ray diffraction | B | — | — |
| 3BZD | Manipulating the coupled folding and binding process drives affinity maturation in a… | x-ray diffraction | B | — | — |
| P0A0L5 | AlphaFold monomer V2.0 prediction for enterotoxin type C-3 (P0A0L5) | predicted | A | — | — |
Experiment against prediction
- 3BVZ chain A against the predicted model P0A0L5: TM-score 0.99, RMSD 0.42 Å
- 3BVZ chain A against the predicted model P0A0L5: TM-score 0.99, RMSD 0.42 Å
- 3BVG chain A against the predicted model P0A0L5: TM-score 0.99, RMSD 0.45 Å
- 3BVG chain A against the predicted model P0A0L5: TM-score 0.99, RMSD 0.45 Å
- 1KLU chain D against the predicted model P0A0L5: TM-score 0.99, RMSD 0.47 Å
- 1KLU chain D against the predicted model P0A0L5: TM-score 0.99, RMSD 0.47 Å
- 3BVM chain A against the predicted model P0A0L5: TM-score 0.99, RMSD 0.47 Å
- 3BVM chain A against the predicted model P0A0L5: TM-score 0.99, RMSD 0.47 Å
- 1SJH chain D against the predicted model P0A0L5: TM-score 0.99, RMSD 0.49 Å
- 1SJH chain D against the predicted model P0A0L5: TM-score 0.99, RMSD 0.49 Å
Elsewhere
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