MolNFT v1 · #11647 · protein
Native L-aspartate ammonia lyase
1JSW · L-aspartate ammonia-lyase: “Native L-aspartate ammonia lyase”. X-ray diffraction, 1 ligand (BGC), 20 pockets (best druggability 0.82). MolNFT v1 #11647 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1JSW
- Type
- protein
- Length
- 1,791 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-aspartate ammonia-lyase
- EC
- 4.3.1.1
- UniProt
- P0AC38
- Ligands
- BGC
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 3 distinct chains · 56% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | L-aspartate ammonia-lyase (EC 4.3.1.1) | protein | 459 | 58% helix, 6% strand | P0AC38 |
| B | L-aspartate ammonia-lyase (EC 4.3.1.1) | protein | 460 | 55% helix, 5% strand | P0AC38 |
| C | L-aspartate ammonia-lyase (EC 4.3.1.1) | protein | 413 | 55% helix, 8% strand | P0AC38 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 2 copies · chains A, C, B
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 431 | 0.82 | 0.90 | 52 | empty |
| 2 | 457 | 0.79 | 0.87 | 51 | empty |
| 3 | 105 | 0.78 | 0.98 | 25 | empty |
| 4 | 103 | 0.78 | 0.98 | 26 | empty |
| 5 | 786 | 0.77 | 0.81 | 73 | empty |
Interfaces
6 interfaces between chains.
- A–D · 2709 Ų buried · 30 hydrogen bonds · protein-protein
- B–D · 2679 Ų buried · 40 hydrogen bonds · protein-protein
- B–C · 2667 Ų buried · 24 hydrogen bonds · protein-protein
- A–C · 2567 Ų buried · 36 hydrogen bonds · protein-protein
- A–B · 1901 Ų buried · 35 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 P0AC38
- Elsewhere: RCSB PDB 1JSW · PDBe 1JSW · UniProt P0AC38
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