Research workbench
Joint-functions of protein residues and NADP(H) in oxygen-activation by flavin-containing monooxygenase: ASN78LYS mutant
Analyse Joint-functions of protein residues and NADP(H) in oxygen-activation by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XLS
- Type
- protein
- Length
- 1,787 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flavin-containing monooxygenase
- EC
- 1.14.13.8
- UniProt
- Q83XK4
- Ligands
- FAD, NAP
- Pockets
- 16 · best druggability 0.91
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flavin-containing monooxygenase (EC 1.14.13.8) | protein | 446 | 31% helix, 21% strand | Q83XK4 |
| B, C, D | Flavin-containing monooxygenase (EC 1.14.13.8) | protein | 447 | 31% helix, 21% strand | Q83XK4 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, B, C, D
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 4 copies · chains A, B, C, D
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 3 copies · chains A, C, B, D
- PEG · Di(hydroxyethyl)ether · additive · chains A, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1067 | 0.91 | 0.94 | 133 | FAD |
| 2 | 1159 | 0.90 | 0.93 | 132 | FAD |
| 3 | 616 | 0.75 | 0.82 | 55 | empty |
| 4 | 578 | 0.75 | 0.82 | 51 | EPE |
| 5 | 95 | 0.51 | 0.83 | 16 | empty |
Interfaces
5 interfaces between chains.
- A–D · 1917 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 1911 Ų buried · 16 hydrogen bonds · protein-protein
- A–C · 305 Ų buried · 4 hydrogen bonds · protein-protein
- B–D · 296 Ų buried · 4 hydrogen bonds · protein-protein
- A–B · 202 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2XLS · Joint-functions of protein residues and NADP(H) in oxygen-activation by flavin-containing… · 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 Q83XK4
- Elsewhere: RCSB PDB 2XLS · PDBe 2XLS · UniProt Q83XK4
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