Research workbench
Secreted chorismate mutase from mycobacterium tuberculosis
Analyse Secreted chorismate mutase from mycobacterium tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2FP1
- Type
- protein
- Length
- 329 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chorismate mutase
- EC
- 5.4.99.5
- UniProt
- O07746
- Ligands
- PB
- Pockets
- 4 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chorismate mutase (EC 5.4.99.5) | protein | 165 | 73% helix, 0% strand | O07746 |
| B | Chorismate mutase (EC 5.4.99.5) | protein | 164 | 76% helix, 0% strand | O07746 |
Ligands and binding sites
- PB · Lead (II) ion · metal · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 77 | 0.68 | 0.94 | 17 | empty |
| 2 | 222 | 0.60 | 0.81 | 25 | empty |
| 3 | 87 | 0.39 | 0.77 | 19 | empty |
| 4 | 105 | 0.37 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 845 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 2FP1 · Secreted Chorismate Mutase from Mycobacterium tuberculosis · 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 O07746
- Elsewhere: RCSB PDB 2FP1 · PDBe 2FP1 · UniProt O07746
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