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Crystal structure of intact ahpf
Analyse Crystal structure of intact ahpf in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HYU
- Type
- protein
- Length
- 521 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alkyl hydroperoxide reductase subunit F
- EC
- 1.8.1.-
- UniProt
- P19480
- Ligands
- FAD, SO4, CL
- Pockets
- 6 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alkyl hydroperoxide reductase subunit F (EC 1.8.1.-) | protein | 521 | 31% helix, 26% strand | P19480 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1161 | 0.84 | 0.85 | 101 | CL, FAD |
| 2 | 146 | 0.53 | 0.80 | 28 | empty |
| 3 | 133 | 0.53 | 0.81 | 19 | empty |
| 4 | 134 | 0.49 | 0.79 | 25 | empty |
| 5 | 100 | 0.39 | 0.76 | 17 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
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 P19480
- Elsewhere: RCSB PDB 1HYU · PDBe 1HYU · UniProt P19480
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