MolNFT v1 · #150461 · protein
Siderophore hydrolase estb from aspergillus fumigatus
6GUD: “Siderophore hydrolase estb from aspergillus fumigatus”. X-ray diffraction, 2 ligands (SO4, CO3). MolNFT v1 #150461 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6GUD
- Type
- protein
- Length
- 563 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q4WF29
- Ligands
- SO4, CO3
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 282 | — | Q4WF29 |
| B | — | protein | 281 | — | 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.
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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