Research workbench
Crystal structure of chorismate mutase from burkholderia thailandensis
Analyse Crystal structure of chorismate mutase from burkholderia thailandensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CNZ
- Type
- protein
- Length
- 964 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chorismate mutase
- EC
- 5.4.99.5
- UniProt
- A0A1B4JXW9
- Ligands
- NO3
- Pockets
- 10 · best druggability 0.75
Structure
x-ray diffraction · 6 distinct chains · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chorismate mutase (EC 5.4.99.5) | protein | 161 | 76% helix, 0% strand | A0A1B4JXW9 |
| B | Chorismate mutase (EC 5.4.99.5) | protein | 162 | 78% helix, 0% strand | A0A1B4JXW9 |
| C | Chorismate mutase (EC 5.4.99.5) | protein | 163 | 75% helix, 0% strand | A0A1B4JXW9 |
| D | Chorismate mutase (EC 5.4.99.5) | protein | 160 | 78% helix, 0% strand | A0A1B4JXW9 |
| E | Chorismate mutase (EC 5.4.99.5) | protein | 160 | 79% helix, 0% strand | A0A1B4JXW9 |
| F | Chorismate mutase (EC 5.4.99.5) | protein | 158 | 79% helix, 0% strand | A0A1B4JXW9 |
Ligands and binding sites
- NO3 · Nitrate ion · ion · 19 copies · chains A, B, C, D, E, F
- EDO · 1,2-ethanediol · additive · 7 copies · chains B, C, D, A, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 93 | 0.75 | 0.96 | 19 | NO3 |
| 2 | 460 | 0.75 | 0.83 | 65 | NO3, EDO |
| 3 | 91 | 0.74 | 0.96 | 18 | NO3, EDO |
| 4 | 104 | 0.73 | 0.94 | 19 | NO3 |
| 5 | 520 | 0.73 | 0.81 | 60 | EDO |
Interfaces
6 interfaces between chains.
- B–C · 1279 Ų buried · 9 hydrogen bonds · protein-protein
- A–E · 1277 Ų buried · 14 hydrogen bonds · protein-protein
- D–F · 1232 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 279 Ų buried · 2 hydrogen bonds · protein-protein
- B–E · 230 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 6CNZ · Crystal Structure of Chorismate Mutase from Burkholderia thailandensis · 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 A0A1B4JXW9
- Elsewhere: RCSB PDB 6CNZ · PDBe 6CNZ · UniProt A0A1B4JXW9
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