Research workbench
Pmsf-inhibited carboxylesterase from pseudomonas fluorescens
Analyse Pmsf-inhibited carboxylesterase from pseudomonas fluorescens in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AUR
- Type
- protein
- Length
- 436 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carboxylesterase
- EC
- 3.1.1.1
- UniProt
- Q53547
- Ligands
- PMS
- Pockets
- 1 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Carboxylesterase (EC 3.1.1.1) | protein | 218 | 35% helix, 23% strand | Q53547 |
Ligands and binding sites
- PMS · phenylmethanesulfonic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 646 | 0.72 | 0.79 | 56 | PMS |
Interfaces
1 interface between chains.
- A–B · 679 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
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 Q53547
- Elsewhere: RCSB PDB 1AUR · PDBe 1AUR · UniProt Q53547
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