Research workbench
Siderophore hydrolase estb from aspergillus fumigatus
Analyse Siderophore hydrolase estb from aspergillus fumigatus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GUD
- Type
- protein
- Length
- 563 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Siderophore esterase iroe-like, putative
- UniProt
- Q4WF29
- Ligands
- SO4, CO3
- Pockets
- 6 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Siderophore esterase iroe-like, putative | protein | 282 | 43% helix, 21% strand | Q4WF29 |
| B | Siderophore esterase iroe-like, putative | protein | 281 | 44% helix, 21% strand | Q4WF29 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 5 copies · chains A, B
- CO3 · Carbonate ion · ion · 4 copies · chains A, B
- GOL · Glycerol · additive · 7 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 442 | 0.69 | 0.80 | 55 | SO4, CO3 |
| 2 | 430 | 0.67 | 0.79 | 52 | SO4 |
| 3 | 136 | 0.59 | 0.84 | 24 | GOL |
| 4 | 128 | 0.58 | 0.84 | 23 | GOL |
| 5 | 59 | 0.40 | 0.80 | 24 | CO3 |
Interfaces
1 interface between chains.
- A–B · 2064 Ų buried · 40 hydrogen bonds · protein-protein
Compared structures
- 6GUD · Siderophore hydrolase EstB from Aspergillus fumigatus · 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 6GUD · PDBe 6GUD · UniProt Q4WF29
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