Research workbench
Processed aspartate decarboxylase mutant with ASN72 mutated to ala
Analyse Processed aspartate decarboxylase mutant with ASN72 mutated to ala in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TM7
- Type
- protein
- Length
- 245 residues
- Chains
- 4
- 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
- P0A790
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.29
Structure
x-ray diffraction · 4 distinct chains · 13% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aspartate 1-decarboxylase beta chain (EC 4.1.1.11) | protein | 26 | 0% helix, 62% strand | P0A790 |
| B | Aspartate 1-decarboxylase alpha chain (EC 4.1.1.11) | protein | 94 | 17% helix, 45% strand | P0A790 |
| C | Aspartate 1-decarboxylase beta chain (EC 4.1.1.11) | protein | 24 | 0% helix, 67% strand | P0A790 |
| D | Aspartate 1-decarboxylase alpha chain (EC 4.1.1.11) | protein | 101 | 16% helix, 43% strand | P0A790 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains B, C, D
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 | 58 | 0.29 | 0.74 | 16 | empty |
Interfaces
6 interfaces between chains.
- C–D · 1648 Ų buried · 41 hydrogen bonds · protein-protein
- A–B · 1618 Ų buried · 39 hydrogen bonds · protein-protein
- A–D · 544 Ų buried · 11 hydrogen bonds · protein-protein
- B–D · 483 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 197 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 3TM7 · Processed Aspartate Decarboxylase Mutant with Asn72 mutated to Ala · the same entry in another collection · chain D against D, TM-score 1.00
- P0A790 · AlphaFold monomer V2.0 prediction for aspartate 1-decarboxylase (P0A790) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 3TM7 · PDBe 3TM7 · UniProt P0A790
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