Research workbench
Crystal structure of chorismate mutase from burkholderia phymatum
Analyse Crystal structure of chorismate mutase from burkholderia phymatum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TS9
- Type
- protein
- Length
- 1,295 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chorismate mutase
- UniProt
- B2JYH9
- Pockets
- 20 · best druggability 0.72
Structure
x-ray diffraction · 4 distinct chains · 76% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chorismate mutase | protein | 164 | 79% helix, 0% strand | B2JYH9 |
| B, G | Chorismate mutase | protein | 161 | 75% helix, 0% strand | B2JYH9 |
| C, D, E | Chorismate mutase | protein | 161 | 76% helix, 0% strand | B2JYH9 |
| F, H | Chorismate mutase | protein | 163 | 75% helix, 0% strand | B2JYH9 |
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 367 | 0.72 | 0.84 | 51 | empty |
| 2 | 374 | 0.71 | 0.83 | 57 | empty |
| 3 | 206 | 0.69 | 0.86 | 27 | empty |
| 4 | 306 | 0.68 | 0.83 | 46 | empty |
| 5 | 227 | 0.67 | 0.84 | 25 | empty |
Interfaces
7 interfaces between chains.
- A–B · 1095 Ų buried · 13 hydrogen bonds · protein-protein
- E–F · 1091 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 1079 Ų buried · 14 hydrogen bonds · protein-protein
- G–H · 1076 Ų buried · 12 hydrogen bonds · protein-protein
- D–E · 828 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide (disulfide).
Compared structures
- 5TS9 · Crystal structure of Chorismate mutase from Burkholderia phymatum · the same entry in another collection · chain A against A, TM-score 1.00
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 B2JYH9
- Elsewhere: RCSB PDB 5TS9 · PDBe 5TS9 · UniProt B2JYH9
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