Research workbench
Structure of esterase EST22 with P-nitrophenol
Analyse Structure of esterase EST22 with P-nitrophenol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5HC0
- Type
- protein
- Length
- 338 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lipolytic enzyme
- EC
- 3.1.1.-
- UniProt
- H6BDX1
- Ligands
- NPO
- Pockets
- 2 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lipolytic enzyme (EC 3.1.1.-) | protein | 338 | 40% helix, 19% strand | H6BDX1 |
Ligands and binding sites
- NPO · P-nitrophenol · ligand · 2 copies · chains A
- GOL · Glycerol · additive · 4 copies · chains A
- ACY · Acetic acid · additive · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 666 | 0.73 | 0.79 | 43 | GOL, ACY, NPO |
| 2 | 91 | 0.40 | 0.78 | 20 | empty |
Compared structures
- 5HC0 · Structure of esterase Est22 with p-nitrophenol · 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 H6BDX1
- Elsewhere: RCSB PDB 5HC0 · PDBe 5HC0 · UniProt H6BDX1
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