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Crystal structure of pyrrolidone carboxyl peptidase from thermus thermophilus
Analyse Crystal structure of pyrrolidone carboxyl peptidase from thermus thermophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EBJ
- Type
- protein
- Length
- 384 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pyrrolidone carboxyl peptidase
- EC
- 3.4.19.3
- UniProt
- Q5SJW4
- Pockets
- 3 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Pyrrolidone carboxyl peptidase (EC 3.4.19.3) | protein | 192 | 31% helix, 24% strand | Q5SJW4 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 806 | 0.71 | 0.76 | 69 | empty |
| 2 | 86 | 0.37 | 0.76 | 16 | empty |
| 3 | 62 | 0.33 | 0.76 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 625 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 2EBJ · Crystal structure of pyrrolidone carboxyl peptidase from Thermus thermophilus · the same entry in another collection · chain A against A, TM-score 1.00
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 Q5SJW4
- Elsewhere: RCSB PDB 2EBJ · PDBe 2EBJ · UniProt Q5SJW4
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