Research workbench
Serine 25 to threonine mutation of aspartate decarboxylase
Analyse Serine 25 to threonine mutation of aspartate decarboxylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PQH
- Type
- protein
- Length
- 234 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
- NA
- Pockets
- 1 · best druggability 0.28
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 | 119 | 13% helix, 45% strand | P0A790 |
| B | Aspartate 1-decarboxylase (EC 4.1.1.11) | protein | 115 | 14% helix, 48% strand | P0A790 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 61 | 0.28 | 0.74 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 946 Ų buried · 14 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 1PQH · PDBe 1PQH · UniProt P0A790
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