Research workbench
Thermogutta terrifontis esterase 2 phosphorylated by paraoxon
Analyse Thermogutta terrifontis esterase 2 phosphorylated by paraoxon in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BFR
- Type
- protein
- Length
- 260 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Esterase
- EC
- 3.1.1.1
- UniProt
- A0A0X1KHD1
- Ligands
- CO3
- Pockets
- 1 · best druggability 0.38
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Esterase (EC 3.1.1.1) | protein | 260 | 32% helix, 22% strand | A0A0X1KHD1 |
Ligands and binding sites
- CO3 · Carbonate ion · ion · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 108 | 0.38 | 0.75 | 19 | CO3 |
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 7BFR · Thermogutta terrifontis esterase 2 phosphorylated by paraoxon · 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 A0A0X1KHD1
- Elsewhere: RCSB PDB 7BFR · PDBe 7BFR · UniProt A0A0X1KHD1
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