Research workbench
Siderophore hydrolase EstB from Aspergillus fumigatus in complex with TAFC
Analyse Siderophore hydrolase EstB from Aspergillus fumigatus in complex with TAFC in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GUR
- Type
- protein
- Length
- 561 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.1
- Source
- Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
- Molecule
- Siderophore triacetylfusarinine C esterase
- EC
- 3.1.-.-
- UniProt
- Q4WF29
- Ligands
- FN8, FE, CO3
- Pockets
- 4 · best druggability 0.68
Structure
x-ray diffraction · resolution 2.1 · 2 distinct chains · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Siderophore triacetylfusarinine C esterase (EC 3.1.-.-) | protein | 279 | 42% helix, 21% strand | Q4WF29 |
| B | Siderophore triacetylfusarinine C esterase (EC 3.1.-.-) | protein | 282 | 41% helix, 21% strand | Q4WF29 |
Ligands and binding sites
- FN8 · (~{Z})-5-[(1~{S},2~{S})-2-acetamido-1-oxidanyl-5-[oxidanyl(propanoyl)amino]pentoxy]-~{N},3-dimethyl-~{N}-oxidanyl-pent-2-enamide · ligand · 2 copies · chains A, B
- FE · Fe (III) ion · metal · 2 copies
- CO3 · Carbonate ion · ion · 2 copies · chains B
- GOL · Glycerol · additive · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 478 | 0.68 | 0.79 | 52 | FN8, GOL |
| 2 | 404 | 0.66 | 0.79 | 47 | FN8, GOL |
| 3 | 190 | 0.64 | 0.84 | 26 | GOL |
| 4 | 138 | 0.57 | 0.83 | 24 | GOL |
Interfaces
1 interface between chains.
- A–B · 2196 Ų buried · 43 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 6GUR · Siderophore hydrolase estb from aspergillus fumigatus in complex with tafc · the same entry in another collection · chain A against A, TM-score 1.00
- Q4WF29 · AlphaFold monomer V2.0 prediction for siderophore triacetylfusarinine C esterase (Q4WF29) · a predicted model of the same protein · 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 Q4WF29
- Elsewhere: RCSB PDB 6GUR · PDBe 6GUR · UniProt Q4WF29
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