Research workbench
Chorismate lyase with product, 1.0 a resolution
Analyse Chorismate lyase with product, 1.0 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TT8
- Type
- protein
- Length
- 164 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chorismate-pyruvate lyase
- EC
- 4.-.-.-
- UniProt
- P26602
- Ligands
- PHB
- Pockets
- 1 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chorismate-pyruvate lyase (EC 4.-.-.-) | protein | 164 | 24% helix, 38% strand | P26602 |
Ligands and binding sites
- PHB · P-hydroxybenzoic acid · 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 | 50 | 0.70 | 0.98 | 18 | empty |
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 P26602
- Elsewhere: RCSB PDB 1TT8 · PDBe 1TT8 · UniProt P26602
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