Research workbench
Enterobactin hydolase iroe complex with dfp
Analyse Enterobactin hydolase iroe complex with dfp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GZS
- Type
- protein
- Length
- 249 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Iroe protein
- UniProt
- Q6KD95
- Ligands
- DFP
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Iroe protein | protein | 249 | 40% helix, 23% strand | Q6KD95 |
Ligands and binding sites
- DFP · Diisopropyl phosphonate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 4 modified, 1 covalent (engineered, covalent ligand).
Compared structures
- 2GZS · Enterobactin Hydolase IroE Complex with DFP · 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 Q6KD95
- Elsewhere: RCSB PDB 2GZS · PDBe 2GZS · UniProt Q6KD95
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