Research workbench
Snapshots of esterase D from lactobacillus rhamnosus: insights into a rotation driven catalytic mechanism
Analyse Snapshots of esterase D from lactobacillus rhamnosus: insights into a rotation… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DLT
- Type
- protein
- Length
- 239 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Esterase D
- UniProt
- B2CZF3
- Ligands
- BUA
- Pockets
- 2 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Esterase D | protein | 239 | 47% helix, 15% strand | B2CZF3 |
Ligands and binding sites
- BUA · butanoic acid · ligand · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 244 | 0.59 | 0.79 | 32 | BUA |
| 2 | 66 | 0.52 | 0.86 | 19 | empty |
Compared structures
- 3DLT · Snapshots of esterase D from lactobacillus rhamnosus: Insights into a rotation driven… · 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 B2CZF3
- Elsewhere: RCSB PDB 3DLT · PDBe 3DLT · UniProt B2CZF3
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