MolNFT v1 · #89815 · protein
Crystal structure of FAD binding domain of ERV1 from saccharomyces cerevisiae
4E0H · Mitochondrial FAD-linked sulfhydryl oxidase ERV1: “Crystal structure of FAD binding domain of ERV1 from saccharomyces cerevisiae”. X-ray diffraction, 1 ligand (FAD), 1 pocket (best druggability 0.62). MolNFT v1 #89815 on GenesisL1…
- PDB
- 4E0H
- Type
- protein
- Length
- 105 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mitochondrial FAD-linked sulfhydryl oxidase ERV1
- EC
- 1.8.3.2
- UniProt
- P27882
- Ligands
- FAD
- Pockets
- 1 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 70% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mitochondrial FAD-linked sulfhydryl oxidase ERV1 (EC 1.8.3.2) | protein | 105 | 70% helix, 0% strand | P27882 |
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
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 242 | 0.62 | 0.81 | 34 | FAD |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4E0H · Crystal structure of FAD binding domain of Erv1 from Saccharomyces cerevisiae · the same entry in another collection · chain A against A, TM-score 1.00
- P27882 · AlphaFold monomer V2.0 prediction for mitochondrial FAD-linked sulfhydryl oxidase ERV1… · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P27882
- Elsewhere: RCSB PDB 4E0H · PDBe 4E0H · UniProt P27882
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