Research workbench
Structure of escherichia COLI threonine aldolase in complex with allo- thr
Analyse Structure of escherichia COLI threonine aldolase in complex with allo- thr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LNL
- Type
- protein
- Length
- 666 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Low-specificity L-threonine aldolase
- EC
- 4.1.2.5
- UniProt
- E7U392
- Ligands
- PLG, MG, CL
- Pockets
- 4 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Low-specificity L-threonine aldolase (EC 4.1.2.5) | protein | 334 | 44% helix, 18% strand | E7U392 |
| B | Low-specificity L-threonine aldolase (EC 4.1.2.5) | protein | 332 | 45% helix, 18% strand | E7U392 |
Ligands and binding sites
- PLG · N-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane] · ligand · chains B
- MG · Magnesium ion · metal · 3 copies · chains A, B
- CL · Chloride ion · ion · chains A
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 2 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 371 | 0.60 | 0.77 | 57 | PLG |
| 2 | 320 | 0.54 | 0.74 | 42 | empty |
| 3 | 56 | 0.41 | 0.82 | 25 | empty |
| 4 | 65 | 0.30 | 0.74 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1031 Ų buried · 23 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 4LNL · Structure of Escherichia coli Threonine Aldolase in Complex with Allo-Thr · 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 E7U392
- Elsewhere: RCSB PDB 4LNL · PDBe 4LNL · UniProt E7U392
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