MolNFT v1 · #18483 · protein
Glycine 24 to serine mutation of aspartate decarboxylase
1PQF · Aspartate 1-decarboxylase: “Glycine 24 to serine mutation of aspartate decarboxylase”. X-ray diffraction, 1 ligand (SO4), 2 pockets (best druggability 0.57). MolNFT v1 #18483 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 1PQF
- Type
- protein
- Length
- 243 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate 1-decarboxylase
- EC
- 4.1.1.11
- UniProt
- P0A790
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 14% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate 1-decarboxylase (EC 4.1.1.11) | protein | 127 | 14% helix, 47% strand | P0A790 |
| B | Aspartate 1-decarboxylase (EC 4.1.1.11) | protein | 116 | 14% helix, 47% strand | P0A790 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 129 | 0.57 | 0.83 | 25 | empty |
| 2 | 100 | 0.39 | 0.76 | 19 | SO4 |
Interfaces
1 interface between chains.
- A–B · 918 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (oxidation).
Compared structures
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 P0A790
- Elsewhere: RCSB PDB 1PQF · PDBe 1PQF · UniProt P0A790
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