Research workbench
Structure of the engineered retro-aldolase RA95.5-5
Analyse Structure of the engineered retro-aldolase RA95.5-5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4A2R
- Type
- protein
- Length
- 247 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Indole-3-glycerol phosphate synthase
- EC
- 4.1.1.48
- UniProt
- Q06121
- Ligands
- 3NK
- Pockets
- 1 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Indole-3-glycerol phosphate synthase (EC 4.1.1.48) | protein | 247 | 42% helix, 16% strand | Q06121 |
Ligands and binding sites
- 3NK · 1-(6-methoxynaphthalen-2-yl)butane-1,3-dione · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 362 | 0.68 | 0.81 | 40 | 3NK |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
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 Q06121
- Elsewhere: RCSB PDB 4A2R · PDBe 4A2R · UniProt Q06121
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