Research workbench
Structure of guanine nucleotide (gppcp) complex of adenylosuccinate synthetase from escherichia COLI at pH 6.5 and 25 degree celsius
Analyse Structure of guanine nucleotide (gppcp) complex of adenylosuccinate synthetase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HON
- Type
- protein
- Length
- 862 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adenylosuccinate synthetase
- EC
- 6.3.4.4
- UniProt
- P0A7D4
- Ligands
- GNH
- Pockets
- 11 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Adenylosuccinate synthetase (EC 6.3.4.4) | protein | 431 | 35% helix, 20% strand | P0A7D4 |
Ligands and binding sites
- GNH · Aminophosphonic acid-guanylate ester · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 259 | 0.84 | 0.96 | 31 | empty |
| 2 | 104 | 0.77 | 0.97 | 25 | empty |
| 3 | 121 | 0.76 | 0.95 | 24 | empty |
| 4 | 968 | 0.76 | 0.79 | 84 | empty |
| 5 | 1127 | 0.75 | 0.78 | 87 | GNH |
Interfaces
1 interface between chains.
- A–B · 2938 Ų buried · 39 hydrogen bonds · protein-protein
Compared structures
- 1HON · Structure of guanine nucleotide (gppcp) complex of adenylosuccinate synthetase from… · the same entry in another collection · chain A against A, TM-score 1.00
- P0A7D4 · AlphaFold monomer V2.0 prediction for adenylosuccinate synthetase (P0A7D4) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P0A7D4
- Elsewhere: RCSB PDB 1HON · PDBe 1HON · UniProt P0A7D4
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