Research workbench
Thermogutta terrifontis esterase 2 phosphonylated by vx
Analyse Thermogutta terrifontis esterase 2 phosphonylated by vx in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BFO
- Type
- protein
- Length
- 277 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Esterase
- EC
- 3.1.1.1
- UniProt
- A0A0X1KHD1
- Pockets
- 2 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Esterase (EC 3.1.1.1) | protein | 277 | 31% helix, 20% strand | A0A0X1KHD1 |
Ligands and binding sites
- EOH · Ethanol · 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 | 95 | 0.65 | 0.90 | 22 | empty |
| 2 | 88 | 0.34 | 0.74 | 19 | EOH |
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 7BFO · Thermogutta terrifontis esterase 2 phosphonylated by VX · 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 7BFO · PDBe 7BFO · UniProt A0A0X1KHD1
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