Research workbench
Esterase estb from burkholderia gladioli: an esterase with (beta)- lactamase fold.
Analyse Esterase estb from burkholderia gladioli: an esterase with (beta)- lactamase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CI8
- Type
- protein
- Length
- 754 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (carboxylesterase)
- EC
- 3.1.1.1
- UniProt
- Q9KX40
- Pockets
- 7 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Protein (carboxylesterase) (EC 3.1.1.1) | protein | 377 | 35% helix, 19% strand | Q9KX40 |
Ligands and binding sites
- IPA · Isopropyl alcohol · additive · 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, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 369 | 0.73 | 0.84 | 67 | IPA |
| 2 | 342 | 0.73 | 0.84 | 64 | empty |
| 3 | 373 | 0.63 | 0.79 | 34 | empty |
| 4 | 277 | 0.60 | 0.79 | 34 | empty |
| 5 | 264 | 0.53 | 0.75 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 515 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 1CI8 · Esterase estb from burkholderia gladioli: an esterase with (beta)-lactamase fold. · the same entry in another collection · chain A against A, TM-score 1.00
- Q9KX40 · AlphaFold monomer V2.0 prediction for esterase estb (Q9KX40) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q9KX40
- Elsewhere: RCSB PDB 1CI8 · PDBe 1CI8 · UniProt Q9KX40
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