UniProt P00778
Alpha-lytic protease (P00778)
Alpha-lytic protease (UniProt P00778), EC 3.4.21.12: 94 experimental structures and 1 predicted model on GenesisL1, 5 ligands bound, 1 pocket. Binding sites, druggability and experiment against prediction (TM-score) in GL1X.
- UniProt
- P00778
- Protein
- Alpha-lytic protease
- EC
- 3.4.21.12
- Experimental structures
- 94
- Predicted models
- 1
- Ligands
- 5
- Pockets
- 1 · 0 records with a druggable one
Structures
95 records of P00778 in the MolNFT archive: 94 experimental, 1 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 1BOQ | Pro region C-terminus: protease active site interactions are critical in catalyzing the folding of… | x-ray diffraction | A | — | — |
| 1BOQ | Pro region C-terminus: protease active site interactions are critical in catalyzing the folding of… | x-ray diffraction | A | — | — |
| 1GBA | Alpha-lytic protease with met 190 replaced by ala and gly 216 replaced by ala | x-ray diffraction | A | — | — |
| 1GBA | Alpha-lytic protease with met 190 replaced by ala and gly 216 replaced by ala | x-ray diffraction | A | — | — |
| 1GBB | Alpha-lytic protease with met 190 replaced by ALA AND GLY 216 replaced by ALA complex with… | x-ray diffraction | A | — | — |
| 1GBB | Alpha-lytic protease with met 190 replaced by ala and gly 216 replaced by ala complex with… | x-ray diffraction | A | — | — |
| 1GBC | Alpha-lytic protease with met 190 replaced by ala and gly 216 replaced by ala complex with… | x-ray diffraction | A | — | — |
| 1GBC | Alpha-lytic protease with met 190 replaced by ala and gly 216 replaced by ala complex with… | x-ray diffraction | A | — | — |
| 1GBD | Alpha-lytic protease with met 190 replaced by ala and gly 216 replaced by ala complex with… | x-ray diffraction | A | — | — |
| 1GBD | Alpha-lytic protease with met 190 replaced by ala and gly 216 replaced by ala complex with… | x-ray diffraction | A | — | — |
| 1GBE | Alpha-lytic protease with met 190 replaced by ala and gly 216 replaced by leu | x-ray diffraction | A | — | — |
| 1GBE | Alpha-lytic protease with met 190 replaced by ala and gly 216 replaced by leu | x-ray diffraction | A | — | — |
| 1GBF | Alpha-lytic protease with met 190 replaced by ala and gly 216 replaced by leu complex with… | x-ray diffraction | A | — | — |
| 1GBF | Alpha-lytic protease with met 190 replaced by ala and gly 216 replaced by leu complex with… | x-ray diffraction | A | — | — |
| 1GBH | Alpha-lytic protease with met 190 replaced by ala and gly 216 replaced by leu complex with… | x-ray diffraction | A | — | — |
| 1GBH | Alpha-lytic protease with met 190 replaced by ala and gly 216 replaced by leu complex with… | x-ray diffraction | A | — | — |
| 1GBI | Alpha-lytic protease with met 190 replaced by ala and gly 216 replaced by leu complex with… | x-ray diffraction | A | — | — |
| 1GBI | Alpha-lytic protease with met 190 replaced by ala and gly 216 replaced by leu complex with… | x-ray diffraction | A | — | — |
| 1GBJ | Alpha-lytic protease with met 190 replaced by ala | x-ray diffraction | A | — | — |
| 1GBJ | Alpha-lytic protease with met 190 replaced by ala | x-ray diffraction | A | — | — |
| 1GBK | Alpha-lytic protease with met 190 replaced by ala complex with methoxysuccinyl-ala-ala-pro-alanine… | x-ray diffraction | A | — | — |
| 1GBK | Alpha-lytic protease with met 190 replaced by ala complex with methoxysuccinyl-ala-ala-pro-alanine… | x-ray diffraction | A | — | — |
| 1GBL | Alpha-lytic protease with met 190 replaced by ala complex with methoxysuccinyl-ala-ala-pro-leucine… | x-ray diffraction | A | — | — |
| 1GBL | Alpha-lytic protease with met 190 replaced by ala complex with methoxysuccinyl-ala-ala-pro-leucine… | x-ray diffraction | A | — | — |
| 1GBM | Alpha-lytic protease with met 190 replaced by ala complex with… | x-ray diffraction | A | — | — |
| 1GBM | Alpha-lytic protease with met 190 replaced by ala complex with… | x-ray diffraction | A | — | — |
| 1P01 | Serine protease mechanism. structure of an inhibitory complex oF ALPHA-LYTIC Protease and a tightly… | x-ray diffraction | A | — | — |
| 1P01 | Serine protease mechanism. structure of an inhibitory complex of alpha-lytic protease and a tightly… | x-ray diffraction | A | — | — |
| 1P02 | Structure analysis of specificity. alpha-lytic protease complexes with analogues of reaction… | x-ray diffraction | A | — | — |
| 1P02 | Structure analysis of specificity. alpha-lytic protease complexes with analogues of reaction… | x-ray diffraction | A | — | — |
| 1P03 | Structure analysis of specificity. alpha-lytic protease complexes with analogues of reaction… | x-ray diffraction | A | — | — |
| 1P03 | Structure analysis of specificity. alpha-lytic protease complexes with analogues of reaction… | x-ray diffraction | A | — | — |
| 1P04 | Structure analysis of specificity. alpha-lytic protease complexes with analogues of reaction… | x-ray diffraction | A | — | — |
| 1P04 | Structure analysis of specificity. alpha-lytic protease complexes with analogues of reaction… | x-ray diffraction | A | — | — |
| 1P05 | Structure analysis of specificity. alpha-lytic protease complexes with analogues of reaction… | x-ray diffraction | A | — | — |
| 1P05 | Structure analysis of specificity. alpha-lytic protease complexes with analogues of reaction… | x-ray diffraction | A | — | — |
| 1P06 | Structure analysis of specificity. alpha-lytic protease complexes with analogues of reaction… | x-ray diffraction | A | — | — |
| 1P06 | Structure analysis of specificity. alpha-lytic protease complexes with analogues of reaction… | x-ray diffraction | A | — | — |
| 1P09 | Structural plasticity as a determinant of enzyme specificity. creating broadly specific proteases | x-ray diffraction | A | — | — |
| 1P09 | Structural plasticity as a determinant of enzyme specificity. creating broadly specific proteases | x-ray diffraction | A | — | — |
| 1P10 | Structural plasticity as a determinant of enzyme specificity. creating broadly specific proteases | x-ray diffraction | A | — | — |
| 1P10 | Structural plasticity as a determinant of enzyme specificity. creating broadly specific proteases | x-ray diffraction | A | — | — |
| 1P11 | Crystal structures of alpha-lytic protease complexes with irreversibly bound phosphonate esters | x-ray diffraction | E | — | — |
| 1P11 | Crystal structures of alpha-lytic protease complexes with irreversibly bound phosphonate esters | x-ray diffraction | E | — | — |
| 1P12 | Crystal structures of alpha-lytic protease complexes with irreversibly bound phosphonate esters | x-ray diffraction | E | — | — |
| 1P12 | Crystal structures of alpha-lytic protease complexes with irreversibly bound phosphonate esters | x-ray diffraction | E | — | — |
| 1QQ4 | Crystal structure of an alpha-lytic protease mutant with accelerated folding kinetics, R102H/G134S | x-ray diffraction | A | — | — |
| 1QQ4 | Crystal structure of an alpha-lytic protease mutant with accelerated folding kinetics, R102H/G134S | x-ray diffraction | A | — | — |
| 1QRW | Crystal structure of an alpha-lytic protease mutant with accelerated folding kinetics, R102H/G134S… | x-ray diffraction | A | — | — |
| 1QRW | Crystal structure of an alpha-lytic protease mutant with accelerated folding kinetics, R102H/G134S… | x-ray diffraction | A | — | — |
| 1QRX | Crystal structure of wild-type alpha-lytic protease at 1.6 a, pH 5.14 | x-ray diffraction | A | — | — |
| 1QRX | Crystal structure of wild-type alpha-lytic protease at 1.6 a, pH 5.14 | x-ray diffraction | A | — | — |
| 1SSX | 0.83A resolution crystal structure of alpha-lytic protease at pH 8 | x-ray diffraction | A | — | — |
| 1SSX | 0.83A resolution crystal structure of alpha-lytic protease at pH 8 | x-ray diffraction | A | — | — |
| 1TAL | Alpha-lytic protease at 120 K (single structure model) | x-ray diffraction | A | — | — |
| 1TAL | Alpha-lytic protease at 120 K (single structure model) | x-ray diffraction | A | — | — |
| 2ALP | Refined structure of alpha-lytic protease at 1.7 ångströms resolution. analysis of hydrogen bonding… | x-ray diffraction | A | — | — |
| 2ALP | Refined structure of alpha-lytic protease at 1.7 ångströms resolution. analysis of hydrogen bonding… | x-ray diffraction | A | — | — |
| 2H5C | 0.82A resolution crystal structure of alpha-lytic protease at pH 5 | x-ray diffraction | A | — | — |
| 2H5C | 0.82A resolution crystal structure of alpha-lytic protease at pH 5 | x-ray diffraction | A | — | — |
35 records more on the page itself.
Ligands
Experiment against prediction
- 2ALP chain A against the predicted model P00778: TM-score 1.00, RMSD 0.17 Å
- 2ALP chain A against the predicted model P00778: TM-score 1.00, RMSD 0.17 Å
- 3M7T chain A against the predicted model P00778: TM-score 1.00, RMSD 0.17 Å
- 3M7T chain A against the predicted model P00778: TM-score 1.00, RMSD 0.17 Å
- 3URD chain A against the predicted model P00778: TM-score 1.00, RMSD 0.18 Å
- 3URD chain A against the predicted model P00778: TM-score 1.00, RMSD 0.18 Å
- 3URC chain A against the predicted model P00778: TM-score 1.00, RMSD 0.18 Å
- 3URC chain A against the predicted model P00778: TM-score 1.00, RMSD 0.18 Å
- 1P02 chain A against the predicted model P00778: TM-score 1.00, RMSD 0.19 Å
- 1P02 chain A against the predicted model P00778: TM-score 1.00, RMSD 0.19 Å
Elsewhere
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