Research workbench
X-ray structure of galt-like protein from arabidopsis thaliana AT5G18200
Analyse X-ray structure of galt-like protein from arabidopsis thaliana AT5G18200 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZWJ
- Type
- protein
- Length
- 600 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative galactose-1-phosphate uridyl transferase
- UniProt
- Q9FK51
- Ligands
- ZN
- Pockets
- 4 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative galactose-1-phosphate uridyl transferase | protein | 301 | 33% helix, 24% strand | Q9FK51 |
| B | Putative galactose-1-phosphate uridyl transferase | protein | 299 | 31% helix, 24% strand | Q9FK51 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 665 | 0.81 | 0.85 | 73 | empty |
| 2 | 347 | 0.59 | 0.76 | 42 | empty |
| 3 | 327 | 0.59 | 0.77 | 39 | empty |
| 4 | 57 | 0.33 | 0.77 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1978 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
- 1ZWJ · X-ray structure of galt-like protein from arabidopsis thaliana AT5G18200 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9FK51 · AlphaFold monomer V2.0 prediction for ADP-glucose phosphorylase (Q9FK51) · a predicted model of the same protein · chain A 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 Q9FK51
- Elsewhere: RCSB PDB 1ZWJ · PDBe 1ZWJ · UniProt Q9FK51
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