MolNFT v1 · #105928 · protein
Crystal structure of E. COLI L-threonine aldolase in complex with a non-covalently uncleaved bound L-serine substrate
4RJY · Low specificity L-threonine aldolase: “Crystal structure of E. COLI L-threonine aldolase in complex with a non-covalently uncleaved bound L-serine…”. X-ray diffraction, 2 ligands (SER, NA), 11 pockets (best druggability 0.65).…
- PDB
- 4RJY
- Type
- protein
- Length
- 1,328 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Low specificity L-threonine aldolase
- UniProt
- L4EJM2
- Ligands
- SER, NA
- Pockets
- 11 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Low specificity L-threonine aldolase | protein | 332 | 41% helix, 18% strand | L4EJM2 |
Ligands and binding sites
- SER · Serine · ligand · 4 copies · chains A, B, D, C
- NA · Sodium ion · metal · 6 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 427 | 0.65 | 0.78 | 52 | SER |
| 2 | 440 | 0.62 | 0.76 | 42 | SER |
| 3 | 350 | 0.59 | 0.76 | 36 | SER |
| 4 | 295 | 0.57 | 0.77 | 35 | SER |
| 5 | 62 | 0.47 | 0.84 | 17 | empty |
Interfaces
6 interfaces between chains.
- C–D · 1924 Ų buried · 27 hydrogen bonds · protein-protein
- A–B · 1915 Ų buried · 27 hydrogen bonds · protein-protein
- A–D · 1000 Ų buried · 21 hydrogen bonds · protein-protein
- B–C · 992 Ų buried · 19 hydrogen bonds · protein-protein
- B–D · 951 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (cofactor).
Compared structures
- 4RJY · Crystal structure of E. coli L-Threonine Aldolase in complex with a non-covalently… · the same entry in another collection · chain C against C, 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 L4EJM2
- Elsewhere: RCSB PDB 4RJY · PDBe 4RJY · UniProt L4EJM2
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