Research workbench
Epsp synthase from acinetobacter baumannii
Analyse Epsp synthase from acinetobacter baumannii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5BS5
- Type
- protein
- Length
- 881 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-phosphoshikimate 1-carboxyvinyltransferase
- EC
- 2.5.1.19
- UniProt
- A3M705
- Pockets
- 3 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) | protein | 441 | 31% helix, 28% strand | A3M705 |
| B | 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) | protein | 440 | 31% helix, 29% strand | A3M705 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 618 | 0.64 | 0.75 | 51 | empty |
| 2 | 356 | 0.55 | 0.75 | 41 | empty |
| 3 | 166 | 0.47 | 0.76 | 37 | empty |
Interfaces
1 interface between chains.
- A–B · 675 Ų buried · 4 hydrogen bonds · protein-protein
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 A3M705
- Elsewhere: RCSB PDB 5BS5 · PDBe 5BS5 · UniProt A3M705
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