Research workbench
Lysine decarboxylase a from pseudomonas aeruginosa
Analyse Lysine decarboxylase a from pseudomonas aeruginosa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Q6I
- Type
- protein
- Length
- 749 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Biodegradative arginine decarboxylase
- EC
- 4.1.1.19, 4.1.1.18
- UniProt
- A0A071KXD7
- Ligands
- PLP
- Pockets
- 8 · best druggability 0.65
Structure
electron microscopy · 1 distinct chain · 28% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Biodegradative arginine decarboxylase (EC 4.1.1.19, 4.1.1.18) | protein | 749 | 28% helix, 12% strand | A0A071KXD7 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 218 | 0.65 | 0.83 | 38 | PLP |
| 2 | 376 | 0.61 | 0.77 | 44 | empty |
| 3 | 199 | 0.52 | 0.78 | 27 | empty |
| 4 | 80 | 0.50 | 0.83 | 24 | empty |
| 5 | 110 | 0.48 | 0.80 | 22 | empty |
Modifications
Observed in the structure: 1 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 6Q6I · Lysine decarboxylase A from Pseudomonas aeruginosa · 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 A0A071KXD7
- Elsewhere: RCSB PDB 6Q6I · PDBe 6Q6I · UniProt A0A071KXD7
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