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Structure of phospho-2-dehydro-3-deoxyheptonate aldolase from francisella tularensis schu S4
Analyse Structure of phospho-2-dehydro-3-deoxyheptonate aldolase from francisella… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TQK
- Type
- protein
- Length
- 341 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phospho-2-dehydro-3-deoxyheptonate aldolase
- EC
- 2.5.1.54
- UniProt
- Q5NG89
- Ligands
- MN, CA
- Pockets
- 3 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phospho-2-dehydro-3-deoxyheptonate aldolase (EC 2.5.1.54) | protein | 341 | 41% helix, 18% strand | Q5NG89 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · chains A
- CA · Calcium ion · metal · chains A
- ACT · Acetate ion · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 270 | 0.60 | 0.79 | 43 | ACT |
| 2 | 109 | 0.47 | 0.79 | 22 | empty |
| 3 | 83 | 0.41 | 0.78 | 16 | empty |
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 3TQK · Structure of Phospho-2-dehydro-3-deoxyheptonate aldolase from Francisella tularensis SCHU… · the same entry in another collection · 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 Q5NG89
- Elsewhere: RCSB PDB 3TQK · PDBe 3TQK · UniProt Q5NG89
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