Research workbench
Crystal structure of L-aspartate-alpha-decarboxylase
Analyse Crystal structure of L-aspartate-alpha-decarboxylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1VC3
- Type
- protein
- Length
- 119 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-aspartate-alpha-decarboxylase light chain; L-aspartate-alpha-decarboxylase heavy chain
- EC
- 4.1.1.1
- UniProt
- Q5SKN7
- Ligands
- PYR
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-aspartate-alpha-decarboxylase light chain (EC 4.1.1.1) | protein | 24 | 0% helix, 63% strand | Q5SKN7 |
| B | L-aspartate-alpha-decarboxylase heavy chain (EC 4.1.1.1) | protein | 95 | 17% helix, 44% strand | — |
Ligands and binding sites
- PYR · Pyruvic acid · ligand · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1598 Ų buried · 30 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
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 Q5SKN7
- Elsewhere: RCSB PDB 1VC3 · PDBe 1VC3 · UniProt Q5SKN7
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