Research workbench
Aeromonas jandaei L-allo-threonine aldolase H128Y/S292R double mutant
Analyse Aeromonas jandaei L-allo-threonine aldolase H128Y/S292R double mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3WGC
- Type
- protein
- Length
- 1,310 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-allo-threonine aldolase
- EC
- 4.1.2.49
- UniProt
- O07051
- Ligands
- PLG
- Pockets
- 11 · best druggability 0.77
Structure
x-ray diffraction · 4 distinct chains · 45% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-allo-threonine aldolase (EC 4.1.2.49) | protein | 321 | 45% helix, 17% strand | O07051 |
| B | L-allo-threonine aldolase (EC 4.1.2.49) | protein | 333 | 44% helix, 18% strand | O07051 |
| C | L-allo-threonine aldolase (EC 4.1.2.49) | protein | 325 | 45% helix, 17% strand | O07051 |
| D | L-allo-threonine aldolase (EC 4.1.2.49) | protein | 331 | 45% helix, 18% strand | O07051 |
Ligands and binding sites
- PLG · N-glycine-[3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-yl-methane] · ligand · 4 copies · chains A, C, B, 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 | 820 | 0.77 | 0.80 | 89 | PLG |
| 2 | 526 | 0.75 | 0.83 | 72 | PLG |
| 3 | 451 | 0.74 | 0.84 | 60 | PLG |
| 4 | 359 | 0.69 | 0.82 | 47 | PLG |
| 5 | 77 | 0.45 | 0.82 | 18 | empty |
Interfaces
6 interfaces between chains.
- B–D · 1887 Ų buried · 29 hydrogen bonds · protein-protein
- A–C · 1882 Ų buried · 28 hydrogen bonds · protein-protein
- C–D · 918 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 907 Ų buried · 20 hydrogen bonds · protein-protein
- B–C · 548 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 3WGC · Aeromonas jandaei L-allo-threonine aldolase H128Y/S292R double mutant · the same entry in another collection · chain A against A, TM-score 1.00
- O07051 · AlphaFold monomer V2.0 prediction for L-allo-threonine aldolase (O07051) · a predicted model of the same protein · chain B 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 O07051
- Elsewhere: RCSB PDB 3WGC · PDBe 3WGC · UniProt O07051
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