Research workbench
Siderophore hydrolase esta from aspergillus nidulans
Analyse Siderophore hydrolase esta from aspergillus nidulans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GUO
- Type
- protein
- Length
- 1,195 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q5AV79
- Ligands
- CL
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 297 | — | Q5AV79 |
| B | — | protein | 297 | — | Q5AV79 |
| C | — | protein | 298 | — | Q5AV79 |
| D | — | protein | 303 | — | Q5AV79 |
Ligands and binding sites
- CL · Chloride ion · ion · 6 copies · chains A, B, C, D
- PGE · Triethylene glycol · additive · 7 copies · chains A, B, C, D
- GOL · Glycerol · additive · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6GUO · Siderophore hydrolase EstA from Aspergillus nidulans · 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 Q5AV79
- Elsewhere: RCSB PDB 6GUO · PDBe 6GUO · UniProt Q5AV79
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