Research workbench
Crystal structure of tripeptidyl peptidase 2 (tpp II)
Analyse Crystal structure of tripeptidyl peptidase 2 (tpp II) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3LXU
- Type
- protein
- Length
- 1,217 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tripeptidyl-peptidase 2
- EC
- 3.4.14.10
- UniProt
- Q9V6K1
- Pockets
- 20 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Tripeptidyl-peptidase 2 (EC 3.4.14.10) | protein | 1217 | 26% helix, 27% strand | Q9V6K1 |
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 466 | 0.80 | 0.88 | 59 | empty |
| 2 | 1086 | 0.79 | 0.80 | 106 | empty |
| 3 | 152 | 0.75 | 0.93 | 33 | empty |
| 4 | 392 | 0.63 | 0.78 | 42 | empty |
| 5 | 305 | 0.61 | 0.78 | 38 | empty |
Modifications
Observed in the structure: 25 modified (engineered).
Compared structures
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 Q9V6K1
- Elsewhere: RCSB PDB 3LXU · PDBe 3LXU · UniProt Q9V6K1
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