Research workbench
Crystal structure of tagatose 1,6-diphosphate aldolase from staphylococcus aureus
Analyse Crystal structure of tagatose 1,6-diphosphate aldolase from staphylococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KAO
- Type
- protein
- Length
- 325 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tagatose 1,6-diphosphate aldolase
- EC
- 4.1.2.40
- UniProt
- P0A009
- Ligands
- ZN, SO4
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tagatose 1,6-diphosphate aldolase (EC 4.1.2.40) | protein | 325 | 49% helix, 14% strand | P0A009 |
Ligands and binding sites
- ZN · Zinc ion · metal · 3 copies · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
- GOL · Glycerol · additive · 3 copies · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 380 | 0.69 | 0.81 | 43 | SO4, ZN |
| 2 | 153 | 0.48 | 0.77 | 28 | GOL |
| 3 | 51 | 0.40 | 0.82 | 17 | GOL |
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 3KAO · Crystal structure of tagatose 1,6-diphosphate aldolase from Staphylococcus aureus · the same entry in another collection · chain A against A, TM-score 1.00
- P0A009 · AlphaFold monomer V2.0 prediction for tagatose 1,6-diphosphate aldolase (P0A009) · 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 P0A009
- Elsewhere: RCSB PDB 3KAO · PDBe 3KAO · UniProt P0A009
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