MolNFT v1 · #27705 · protein
Crystal structure of active site F1-mutant E213Q soaked with peptide pro-leu-gly-gly
1XRP · Proline iminopeptidase: “Crystal structure of active site F1-mutant E213Q soaked with peptide pro-leu-gly-gly”. X-ray diffraction, 1 ligand (PRO), 3 pockets (best druggability 0.73). MolNFT v1 #27705 on GenesisL1: 3D structure…
- PDB
- 1XRP
- Type
- protein
- Length
- 294 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proline iminopeptidase; Plgg
- EC
- 3.4.11.5
- UniProt
- P96084
- Ligands
- PRO
- Pockets
- 3 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proline iminopeptidase (EC 3.4.11.5) | protein | 290 | 47% helix, 19% strand | P96084 |
| Q | Plgg | protein | 4 | 0% helix, 0% strand | — |
Ligands and binding sites
- PRO · Proline · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 53 | 0.73 | 0.99 | 19 | PRO |
| 2 | 63 | 0.30 | 0.74 | 15 | empty |
| 3 | 52 | 0.29 | 0.75 | 16 | empty |
Interfaces
1 interface between chains.
- A–Q · 307 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1XRP · Crystal structure of active site F1-mutant E213Q soaked with peptide Pro-Leu-Gly-Gly · the same entry in another collection · chain A against A, TM-score 1.00
- P96084 · AlphaFold monomer V2.0 prediction for proline iminopeptidase (P96084) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P96084
- Elsewhere: RCSB PDB 1XRP · PDBe 1XRP · UniProt P96084
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.