Research workbench
Providencia stuartii arginine decarboxylase (adc), decamer structure
Analyse Providencia stuartii arginine decarboxylase (adc), decamer structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7P9B
- Type
- protein
- Length
- 7,550 residues
- Chains
- 10
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Biodegradative arginine decarboxylase
- EC
- 4.1.1.19
- UniProt
- A0A379GV98
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 1 distinct chain · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J | Biodegradative arginine decarboxylase (EC 4.1.1.19) | protein | 755 | 41% helix, 17% strand | A0A379GV98 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1012 | 0.83 | 0.84 | 101 | empty |
| 2 | 1101 | 0.83 | 0.84 | 108 | empty |
| 3 | 1157 | 0.81 | 0.82 | 101 | empty |
| 4 | 1181 | 0.81 | 0.82 | 97 | empty |
| 5 | 1177 | 0.81 | 0.82 | 99 | empty |
Interfaces
20 interfaces between chains.
- G–H · 5298 Ų buried · 81 hydrogen bonds · protein-protein
- E–F · 5291 Ų buried · 70 hydrogen bonds · protein-protein
- A–B · 5281 Ų buried · 79 hydrogen bonds · protein-protein
- I–J · 5271 Ų buried · 75 hydrogen bonds · protein-protein
- C–D · 5247 Ų buried · 69 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (cofactor).
Compared structures
- 7P9B · Providencia stuartii Arginine decarboxylase (Adc), decamer structure · 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 A0A379GV98
- Elsewhere: RCSB PDB 7P9B · PDBe 7P9B · UniProt A0A379GV98
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