UniProt P42575
Caspase-2 (P42575)
Caspase-2 (UniProt P42575), EC 3.4.22.55: 22 experimental structures and 1 predicted model on GenesisL1, 1 ligand bound, 5 pockets. Binding sites, druggability and experiment against prediction (TM-score) in GL1X.
- UniProt
- P42575
- Protein
- Caspase-2
- EC
- 3.4.22.55
- Experimental structures
- 22
- Predicted models
- 1
- Ligands
- 1
- Pockets
- 5 · 2 records with a druggable one
Structures
23 records of P42575 in the MolNFT archive: 22 experimental, 1 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 1PYO | Crystal Structure of Human Caspase-2 in Complex with Acetyl-Leu-Asp-Glu-Ser-Asp-cho | x-ray diffraction | A, B, C, D | — | — |
| 1PYO | Crystal structure of human caspase-2 in complex with acetyl-leu-asp- glu-ser-asp-cho | x-ray diffraction | A, B, C, D | — | — |
| 2P2C | Inhibition of caspase-2 by a designed ankyrin repeat protein (DARPin) | x-ray diffraction | A, B, C, D, E, F, G, H, I, J, K, L | — | — |
| 2P2C | Inhibition of caspase-2 by a designed ankyrin repeat protein (darpin) | x-ray diffraction | A, B, C, D, E, F, G, H, I, J, K, L | — | — |
| 3R5J | Crystal structure of active caspase-2 bound with Ac-ADVAD-CHO | x-ray diffraction | A, B, C, D | — | — |
| 3R5J | Crystal structure of active caspase-2 bound with ac-advad-cho | x-ray diffraction | A, B, C, D | — | — |
| 3R6G | Crystal structure of active caspase-2 bound with Ac-VDVAD-CHO | x-ray diffraction | A, B, C, D | — | — |
| 3R6G | Crystal structure of active caspase-2 bound with ac-vdvad-cho | x-ray diffraction | A, B, C, D | — | — |
| 3R6L | Caspase-2 T380A bound with Ac-VDVAD-CHO | x-ray diffraction | A, B, C, D | — | — |
| 3R6L | Caspase-2 T380A bound with ac-vdvad-cho | x-ray diffraction | A, B, C, D | — | — |
| 3R7B | Caspase-2 bound to one copy of Ac-DVAD-CHO | x-ray diffraction | A, B, C, D | — | — |
| 3R7B | Caspase-2 bound to one copy of ac-dvad-cho | x-ray diffraction | A, B, C, D | — | — |
| 3R7N | Caspase-2 bound with two copies of Ac-DVAD-CHO | x-ray diffraction | A, B, C, D | — | — |
| 3R7N | Caspase-2 bound with two copies of ac-dvad-cho | x-ray diffraction | A, B, C, D | — | — |
| 3R7S | Crystal Structure of Apo Caspase2 | x-ray diffraction | A, B, C, D | — | — |
| 3R7S | Crystal structure of apo CASPASE2 | x-ray diffraction | A, B, C, D | — | — |
| 3RJM | CASPASE2 IN COMPLEX WITH CHDI LIGAND 33c | x-ray diffraction | A, B, C, D | — | — |
| 3RJM | CASPASE2 in complex with chdi ligand 33C | x-ray diffraction | A, B, C, D | — | — |
| 6S9K | Structure of 14-3-3 gamma in complex with caspase-2 peptide containing 14-3-3 binding motif Ser139… | x-ray diffraction | B | CFH | 2 (best 0.61) |
| 6S9K | Structure of 14-3-3 gamma in complex with caspase-2 peptide containing 14-3-3 binding motif SER139… | x-ray diffraction | B | CFH | — |
| 6SAD | Structure of 14-3-3 gamma in complex with double phosphorylated caspase-2 peptide on Ser139 and… | x-ray diffraction | C | — | 3 (best 0.61) |
| 6SAD | Structure of 14-3-3 gamma in complex with double phosphorylated caspase-2 peptide on SER139 and… | x-ray diffraction | C | — | — |
| P42575 | AlphaFold monomer V2.0 prediction for caspase-2 (P42575) | predicted | A | — | — |
Ligands
- CFH · 1,1,1,3,3,3-hexafluoropropan-2-ol · in 2 records
Experiment against prediction
- 3R5J chain C against the predicted model P42575: TM-score 0.99, RMSD 0.45 Å
- 3R5J chain C against the predicted model P42575: TM-score 0.99, RMSD 0.45 Å
- 3R7B chain C against the predicted model P42575: TM-score 0.99, RMSD 0.45 Å
- 3R7B chain C against the predicted model P42575: TM-score 0.99, RMSD 0.45 Å
- 3R6G chain C against the predicted model P42575: TM-score 0.99, RMSD 0.51 Å
- 3R6G chain C against the predicted model P42575: TM-score 0.99, RMSD 0.51 Å
- 3R7N chain A against the predicted model P42575: TM-score 0.99, RMSD 0.48 Å
- 3R7N chain A against the predicted model P42575: TM-score 0.99, RMSD 0.48 Å
- 3R5J chain A against the predicted model P42575: TM-score 0.99, RMSD 0.50 Å
- 3R5J chain A against the predicted model P42575: TM-score 0.99, RMSD 0.50 Å
Elsewhere
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