Research workbench
Flavin monooxygenase from stenotrophomonas maltophilia. Q193R H194T mutant
Analyse Flavin monooxygenase from stenotrophomonas maltophilia. Q193R H194T mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4C5O
- Type
- protein
- Length
- 2,641 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flavin monooxygenase
- EC
- 1.14.13.8
- UniProt
- B2FRL2
- Ligands
- FAD, SO4
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 4 distinct chains · 27% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flavin monooxygenase (EC 1.14.13.8) | protein | 327 | 27% helix, 19% strand | B2FRL2 |
| B, C, E, F, G | Flavin monooxygenase (EC 1.14.13.8) | protein | 330 | 27% helix, 23% strand | B2FRL2 |
| D | Flavin monooxygenase (EC 1.14.13.8) | protein | 333 | 27% helix, 23% strand | B2FRL2 |
| H | Flavin monooxygenase (EC 1.14.13.8) | protein | 331 | 27% helix, 23% strand | B2FRL2 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 8 copies · chains A, B, C, D, E, F, G, H
- SO4 · Sulfate ion · ion · 33 copies · chains A, B, C, D, G, E, F, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 951 | 0.83 | 0.84 | 97 | empty |
| 2 | 1183 | 0.79 | 0.81 | 116 | SO4 |
| 3 | 826 | 0.79 | 0.82 | 71 | FAD |
| 4 | 1009 | 0.79 | 0.81 | 89 | FAD, SO4 |
| 5 | 1020 | 0.79 | 0.80 | 81 | FAD, SO4 |
Interfaces
13 interfaces between chains.
- E–F · 729 Ų buried · 4 hydrogen bonds · protein-protein
- G–H · 728 Ų buried · 5 hydrogen bonds · protein-protein
- C–D · 718 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 681 Ų buried · 0 hydrogen bonds · protein-protein
- E–G · 497 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4C5O · Flavin monooxygenase from Stenotrophomonas maltophilia. Q193R H194T mutant · 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 B2FRL2
- Elsewhere: RCSB PDB 4C5O · PDBe 4C5O · UniProt B2FRL2
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