MolNFT v1 · #1023 · protein
Human argininosuccinate lyase
1AOS: “Human argininosuccinate lyase”. X-ray diffraction, 4 pockets (best druggability 0.46). MolNFT v1 #1023 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1AOS
- Type
- protein
- Length
- 868 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Argininosuccinate lyase
- EC
- 4.3.2.1
- UniProt
- P04424
- Pockets
- 4 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 64% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Argininosuccinate lyase (EC 4.3.2.1) | protein | 434 | 64% helix, 4% strand | P04424 |
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 199 | 0.46 | 0.74 | 27 | empty |
| 2 | 202 | 0.45 | 0.74 | 24 | empty |
| 3 | 80 | 0.34 | 0.75 | 16 | empty |
| 4 | 56 | 0.30 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1855 Ų buried · 24 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 P04424
- Elsewhere: RCSB PDB 1AOS · PDBe 1AOS · UniProt P04424
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