Research workbench
Crystal structure of the phosphonoacetaldehyde hydrolase D12A mutant complexed with magnesium and substrate phosphonoacetaldehyde
Analyse Crystal structure of the phosphonoacetaldehyde hydrolase D12A mutant complexed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SWW
- Type
- protein
- Length
- 514 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphonoacetaldehyde hydrolase
- EC
- 3.11.1.1
- UniProt
- O31156
- Ligands
- POA, MG
- Pockets
- 2 · best druggability 0.39
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Phosphonoacetaldehyde hydrolase (EC 3.11.1.1) | protein | 257 | 55% helix, 9% strand | O31156 |
Ligands and binding sites
- POA · Phosphonoacetaldehyde · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 56 | 0.39 | 0.81 | 18 | empty |
| 2 | 68 | 0.28 | 0.73 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 702 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1SWW · Crystal structure of the phosphonoacetaldehyde hydrolase D12A mutant complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
- O31156 · AlphaFold monomer V2.0 prediction for phosphonoacetaldehyde hydrolase (O31156) · 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 O31156
- Elsewhere: RCSB PDB 1SWW · PDBe 1SWW · UniProt O31156
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