Research workbench
Crystal structure of escherichia COLI adenylosuccinate lyase mutant H171N with bound AMP and fumarate
Analyse Crystal structure of escherichia COLI adenylosuccinate lyase mutant H171N with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PTQ
- Type
- protein
- Length
- 917 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenylosuccinate lyase
- EC
- 4.3.2.2
- UniProt
- P0AB89
- Ligands
- FUM, AMP
- Pockets
- 5 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 63% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adenylosuccinate lyase (EC 4.3.2.2) | protein | 459 | 63% helix, 5% strand | P0AB89 |
| B | Adenylosuccinate lyase (EC 4.3.2.2) | protein | 458 | 63% helix, 5% strand | P0AB89 |
Ligands and binding sites
- FUM · Fumaric acid · ligand · 2 copies · chains A, B
- AMP · Adenosine monophosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 615 | 0.77 | 0.83 | 64 | AMP, FUM |
| 2 | 629 | 0.77 | 0.83 | 57 | FUM, AMP |
| 3 | 167 | 0.43 | 0.74 | 18 | empty |
| 4 | 147 | 0.41 | 0.74 | 17 | empty |
| 5 | 64 | 0.26 | 0.72 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 3498 Ų buried · 60 hydrogen bonds · protein-protein
Compared structures
- 2PTQ · Crystal structure of Escherichia coli adenylosuccinate lyase mutant H171N with bound AMP… · the same entry in another collection · chain A against A, TM-score 1.00
- P0AB89 · AlphaFold monomer V2.0 prediction for adenylosuccinate lyase (P0AB89) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 P0AB89
- Elsewhere: RCSB PDB 2PTQ · PDBe 2PTQ · UniProt P0AB89
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.