Research workbench
Thermogutta terrifontis esterase 2 phosphoramylated by tabun
Analyse Thermogutta terrifontis esterase 2 phosphoramylated by tabun in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7BFT
- Type
- protein
- Length
- 264 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.99
- Source
- Thermogutta terrifontis
- Molecule
- Esterase
- EC
- 3.1.1.1
- UniProt
- A0A0X1KHD1
- Ligands
- PO4
Structure
x-ray diffraction · resolution 1.99 · 1 distinct chain · 32% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Esterase (EC 3.1.1.1) | protein | 264 | 32% helix, 21% strand | A0A0X1KHD1 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 modified (nonstandard).
Compared structures
- 7BFT · Thermogutta terrifontis esterase 2 phosphoramylated by tabun · 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 7BFT · PDBe 7BFT · UniProt A0A0X1KHD1
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