Research workbench
Crystal structure of ESTE5-pmsf (I)
Analyse Crystal structure of ESTE5-pmsf (I) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3H17
- Type
- protein
- Length
- 292 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ESTERASE/LIPASE
- EC
- 3.1.1.-
- UniProt
- Q0GMU2
- Ligands
- PMS
- Pockets
- 1 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ESTERASE/LIPASE (EC 3.1.1.-) | protein | 292 | 42% helix, 16% strand | Q0GMU2 |
Ligands and binding sites
- PMS · phenylmethanesulfonic acid · ligand · chains A
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 | 974 | 0.76 | 0.78 | 55 | PMS |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 3H17 · Crystal structure of EstE5-PMSF (I) · 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 Q0GMU2
- Elsewhere: RCSB PDB 3H17 · PDBe 3H17 · UniProt Q0GMU2
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