MolNFT v1 · #31926 · protein
Structure of imidazolonepropionase from bacillus subtilis
2BB0: “Structure of imidazolonepropionase from bacillus subtilis”. X-ray diffraction, 1 ligand (ZN), 5 pockets (best druggability 0.72). MolNFT v1 #31926 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2BB0
- Type
- protein
- Length
- 826 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Imidazolonepropionase
- EC
- 3.5.2.7
- UniProt
- P42084
- Ligands
- ZN
- Pockets
- 5 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Imidazolonepropionase (EC 3.5.2.7) | protein | 413 | 36% helix, 25% strand | P42084 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 926 | 0.72 | 0.76 | 73 | empty |
| 2 | 151 | 0.64 | 0.86 | 33 | ACT |
| 3 | 66 | 0.50 | 0.85 | 19 | empty |
| 4 | 185 | 0.49 | 0.77 | 31 | empty |
| 5 | 56 | 0.35 | 0.78 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 305 Ų buried · 5 hydrogen bonds · protein-protein
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 P42084
- Elsewhere: RCSB PDB 2BB0 · PDBe 2BB0 · UniProt P42084
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