Research workbench
T57V mutant of aspartate decarboxylase
Analyse T57V mutant 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
- 4AZD
- Type
- protein
- Length
- 239 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
Structure
x-ray diffraction · 2 distinct chains · 14% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate 1-decarboxylase (EC 4.1.1.11) | protein | 122 | 14% helix, 48% strand | P0A790 |
| B | Aspartate 1-decarboxylase (EC 4.1.1.11) | protein | 117 | 14% helix, 47% strand | P0A790 |
Ligands and binding sites
- MLI · Malonate ion · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1038 Ų buried · 15 hydrogen bonds · protein-protein
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 4AZD · PDBe 4AZD · UniProt P0A790
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