Research workbench
Crystal structure of amylosucrase double mutant A289P-F290I from neisseria polysaccharea.
Analyse Crystal structure of amylosucrase double mutant A289P-F290I from neisseria… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FLQ
- Type
- protein
- Length
- 628 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Amylosucrase
- EC
- 2.4.1.4
- UniProt
- Q9ZEU2
- Pockets
- 3 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Amylosucrase (EC 2.4.1.4) | protein | 628 | 42% helix, 15% strand | Q9ZEU2 |
Ligands and binding sites
- GOL · Glycerol · additive · 7 copies · chains A
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
- PGE · Triethylene glycol · additive · chains A
- PG4 · Tetraethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 426 | 0.77 | 0.86 | 57 | TRS, GOL |
| 2 | 180 | 0.58 | 0.81 | 33 | empty |
| 3 | 73 | 0.40 | 0.80 | 15 | empty |
Compared structures
- 4FLQ · Crystal structure of Amylosucrase double mutant A289P-F290I from Neisseria polysaccharea. · the same entry in another collection · chain A against A, TM-score 1.00
- Q9ZEU2 · AlphaFold monomer V2.0 prediction for amylosucrase (Q9ZEU2) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 Q9ZEU2
- Elsewhere: RCSB PDB 4FLQ · PDBe 4FLQ · UniProt Q9ZEU2
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.