MolNFT v1 · #110399 · protein
Crystal structure of alkylhydroperoxide reductase subunit ahpf from escherichia COLI
4XVG · Alkyl hydroperoxide reductase subunit F: “Crystal structure of alkylhydroperoxide reductase subunit ahpf from escherichia COLI”. X-ray diffraction, 1 ligand (FAD), 5 pockets (best druggability 0.77). MolNFT v1 #110399 on GenesisL1…
- PDB
- 4XVG
- Type
- protein
- Length
- 519 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
- P35340
- Ligands
- FAD
- Pockets
- 5 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alkyl hydroperoxide reductase subunit F (EC 1.8.1.-) | protein | 519 | 33% helix, 27% strand | P35340 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 782 | 0.77 | 0.81 | 77 | FAD |
| 2 | 91 | 0.38 | 0.77 | 17 | empty |
| 3 | 98 | 0.38 | 0.76 | 18 | empty |
| 4 | 61 | 0.30 | 0.75 | 18 | empty |
| 5 | 62 | 0.30 | 0.74 | 14 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4XVG · Crystal structure of Alkylhydroperoxide Reductase Subunit AhpF from Escherichia coli · the same entry in another collection · chain A against A, TM-score 1.00
- P35340 · AlphaFold monomer V2.0 prediction for alkyl hydroperoxide reductase subunit F (P35340) · a predicted model of the same protein · chain A against A, TM-score 0.82
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 P35340
- Elsewhere: RCSB PDB 4XVG · PDBe 4XVG · UniProt P35340
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