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Crystal structure of aspartate decarboxylase, pyruvoly group bound form
Analyse Crystal structure of aspartate decarboxylase, pyruvoly group bound form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UHD
- Type
- protein
- Length
- 119 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aspartate 1-decarboxylase beta chain; Aspartate 1-decarboxylase alpha chain
- EC
- 4.1.1.11
- UniProt
- P56065
- Ligands
- PYR
Structure
x-ray diffraction · 2 distinct chains · 15% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Aspartate 1-decarboxylase beta chain (EC 4.1.1.11) | protein | 24 | 0% helix, 63% strand | P56065 |
| A | Aspartate 1-decarboxylase alpha chain (EC 4.1.1.11) | protein | 95 | 19% helix, 43% strand | P56065 |
Ligands and binding sites
- PYR · Pyruvic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- B–A · 1687 Ų buried · 33 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 1UHD · Crystal structure of aspartate decarboxylase, pyruvoly group bound form · the same entry in another collection · chain B against B, TM-score 1.00
- P56065 · AlphaFold monomer V2.0 prediction for aspartate 1-decarboxylase (P56065) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P56065
- Elsewhere: RCSB PDB 1UHD · PDBe 1UHD · UniProt P56065
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