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Crystal structure of chorismate synthase
Analyse Crystal structure of chorismate synthase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Q1L
- Type
- protein
- Length
- 1,339 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chorismate synthase
- EC
- 4.2.3.5
- UniProt
- O66493
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · 4 distinct chains · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chorismate synthase (EC 4.2.3.5) | protein | 336 | 40% helix, 23% strand | O66493 |
| B | Chorismate synthase (EC 4.2.3.5) | protein | 336 | 41% helix, 21% strand | O66493 |
| C | Chorismate synthase (EC 4.2.3.5) | protein | 333 | 41% helix, 23% strand | O66493 |
| D | Chorismate synthase (EC 4.2.3.5) | protein | 334 | 43% helix, 22% strand | O66493 |
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 873 | 0.86 | 0.89 | 70 | empty |
| 2 | 640 | 0.71 | 0.78 | 62 | empty |
| 3 | 323 | 0.63 | 0.79 | 34 | empty |
| 4 | 297 | 0.60 | 0.79 | 35 | empty |
| 5 | 373 | 0.60 | 0.77 | 47 | empty |
Interfaces
6 interfaces between chains.
- B–C · 4036 Ų buried · 58 hydrogen bonds · protein-protein
- A–D · 3735 Ų buried · 49 hydrogen bonds · protein-protein
- A–C · 1669 Ų buried · 18 hydrogen bonds · protein-protein
- B–D · 1652 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 985 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 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 O66493
- Elsewhere: RCSB PDB 1Q1L · PDBe 1Q1L · UniProt O66493
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