MolNFT v1 · #172566 · protein
Structural characterization of L-proline amide hydrolase from pseudomonas syringae
7A6G · Putative proline iminopeptidase: “Structural characterization of L-proline amide hydrolase from pseudomonas syringae”. X-ray diffraction, 1 ligand (PO4), 1 pocket (best druggability 0.51). MolNFT v1 #172566 on GenesisL1: 3D…
- PDB
- 7A6G
- Type
- protein
- Length
- 303 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative proline iminopeptidase
- UniProt
- A0A0Q0CYJ4
- Ligands
- PO4
- Pockets
- 1 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative proline iminopeptidase | protein | 303 | 43% helix, 17% strand | A0A0Q0CYJ4 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 162 | 0.51 | 0.78 | 19 | empty |
Compared structures
- 7A6G · Structural characterization of L-proline amide hydrolase from Pseudomonas syringae · 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 A0A0Q0CYJ4
- Elsewhere: RCSB PDB 7A6G · PDBe 7A6G · UniProt A0A0Q0CYJ4
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