Research workbench
Structure of mutant pyrrolidone carboxyl peptidase (E192D) from a hyperthermophile, pyrococcus furiosus
Analyse Structure of mutant pyrrolidone carboxyl peptidase (E192D) from a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1X12
- Type
- protein
- Length
- 832 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pyrrolidone-carboxylate peptidase
- EC
- 3.4.19.3
- UniProt
- O73944
- Pockets
- 8 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Pyrrolidone-carboxylate peptidase (EC 3.4.19.3) | protein | 208 | 35% helix, 24% strand | O73944 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 871 | 0.78 | 0.80 | 76 | empty |
| 2 | 1125 | 0.76 | 0.79 | 80 | empty |
| 3 | 81 | 0.37 | 0.76 | 22 | empty |
| 4 | 56 | 0.35 | 0.78 | 17 | empty |
| 5 | 59 | 0.33 | 0.76 | 14 | empty |
Interfaces
6 interfaces between chains.
- B–D · 697 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 691 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 664 Ų buried · 12 hydrogen bonds · protein-protein
- A–D · 651 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 153 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 1X12 · Structure of Mutant Pyrrolidone Carboxyl Peptidase (E192D) from a Hyperthermophile… · the same entry in another collection · chain A against A, TM-score 1.00
- O73944 · AlphaFold monomer V2.0 prediction for pyrrolidone-carboxylate peptidase (O73944) · a predicted model of the same protein · 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 O73944
- Elsewhere: RCSB PDB 1X12 · PDBe 1X12 · UniProt O73944
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