Research workbench
Chorismate mutase from bacillus subtilis at 1.30 ångström
Analyse Chorismate mutase from bacillus subtilis at 1.30 ångström in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1DBF
- Type
- protein
- Length
- 381 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (chorismate mutase)
- EC
- 5.4.99.5
- UniProt
- P19080
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Protein (chorismate mutase) (EC 5.4.99.5) | protein | 127 | 31% helix, 28% strand | P19080 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 9 copies · chains A, B, C
- GOL · Glycerol · additive · 5 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 328 | 0.63 | 0.79 | 40 | SO4, GOL |
| 2 | 332 | 0.59 | 0.77 | 37 | SO4, GOL |
| 3 | 255 | 0.56 | 0.77 | 32 | SO4, GOL |
Interfaces
3 interfaces between chains.
- A–C · 1182 Ų buried · 14 hydrogen bonds · protein-protein
- B–C · 1067 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 1055 Ų buried · 13 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 P19080
- Elsewhere: RCSB PDB 1DBF · PDBe 1DBF · UniProt P19080
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.