Research workbench
Crystal structure of chorismatase at 1.08 ångström resolution.
Analyse Crystal structure of chorismatase at 1.08 ångström resolution. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BPS
- Type
- protein
- Length
- 331 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fkbo
- UniProt
- Q9KID9
- Ligands
- 3EB
- Pockets
- 2 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fkbo | protein | 331 | 25% helix, 35% strand | Q9KID9 |
Ligands and binding sites
- 3EB · 3-(2-carboxyethyl)benzoic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 115 | 0.74 | 0.94 | 31 | 3EB |
| 2 | 93 | 0.34 | 0.74 | 18 | empty |
Modifications
Observed in the structure: 4 modified (engineered).
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 Q9KID9
- Elsewhere: RCSB PDB 4BPS · PDBe 4BPS · UniProt Q9KID9
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