Research workbench
2.5 ångström resolution crystal structure of bifidobacterium longum chorismate synthase
Analyse 2.5 ångström resolution crystal structure of bifidobacterium longum chorismate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4ECD
- Type
- protein
- Length
- 542 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chorismate synthase
- EC
- 4.2.3.5
- UniProt
- B7GS97
- Ligands
- CL
- Pockets
- 7 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chorismate synthase (EC 4.2.3.5) | protein | 274 | 35% helix, 25% strand | B7GS97 |
| B | Chorismate synthase (EC 4.2.3.5) | protein | 268 | 38% helix, 25% strand | B7GS97 |
Ligands and binding sites
- CL · Chloride ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 619 | 0.68 | 0.77 | 63 | empty |
| 2 | 373 | 0.64 | 0.79 | 64 | CL |
| 3 | 72 | 0.54 | 0.86 | 23 | CL |
| 4 | 69 | 0.51 | 0.86 | 22 | empty |
| 5 | 131 | 0.42 | 0.75 | 28 | empty |
Interfaces
1 interface between chains.
- A–B · 1308 Ų buried · 27 hydrogen bonds · protein-protein
Compared structures
- 4ECD · 2.5 Angstrom Resolution Crystal Structure of Bifidobacterium longum Chorismate Synthase · the same entry in another collection · chain A against A, TM-score 1.00
- B7GS97 · AlphaFold monomer V2.0 prediction for chorismate synthase (B7GS97) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 B7GS97
- Elsewhere: RCSB PDB 4ECD · PDBe 4ECD · UniProt B7GS97
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