MolNFT v1 · #35872 · protein
Crystal structure of a mutant pyrrolidone carboxyl peptidase (A199P) from P. furiosus
2EO8 · Pyrrolidone-carboxylate peptidase: “Crystal structure of a mutant pyrrolidone carboxyl peptidase (A199P) from P. furiosus”. X-ray diffraction, 7 pockets (best druggability 0.76). MolNFT v1 #35872 on GenesisL1: 3D structure, binding…
- PDB
- 2EO8
- 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
- 7 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 25% 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, 25% strand | O73944 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1138 | 0.76 | 0.78 | 82 | empty |
| 2 | 968 | 0.76 | 0.78 | 78 | empty |
| 3 | 53 | 0.35 | 0.78 | 17 | empty |
| 4 | 77 | 0.34 | 0.75 | 13 | empty |
| 5 | 71 | 0.32 | 0.74 | 13 | empty |
Interfaces
6 interfaces between chains.
- B–D · 735 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 712 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 680 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 671 Ų buried · 12 hydrogen bonds · protein-protein
- A–D · 111 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 2EO8 · Crystal structure of a mutant pyrrolidone carboxyl peptidase (A199P) from P. furiosus · 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 2EO8 · PDBe 2EO8 · UniProt O73944
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