Research workbench
Crystal structure of wt rntmm
Analyse Crystal structure of wt rntmm in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5IPY
- Type
- protein
- Length
- 890 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flavin-containing monooxygenase
- UniProt
- A3SLM3
- Ligands
- NAP, FAD
- Pockets
- 11 · best druggability 0.91
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Flavin-containing monooxygenase | protein | 445 | 30% helix, 20% strand | A3SLM3 |
Ligands and binding sites
- NAP · Nadp nicotinamide-adenine-dinucleotide phosphate · ligand · 2 copies · chains A, B
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1092 | 0.91 | 0.94 | 137 | FAD |
| 2 | 285 | 0.83 | 0.94 | 50 | empty |
| 3 | 205 | 0.60 | 0.81 | 25 | empty |
| 4 | 127 | 0.47 | 0.78 | 24 | empty |
| 5 | 58 | 0.43 | 0.83 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1817 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 5IPY · Crystal structure of WT RnTmm · 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 A3SLM3
- Elsewhere: RCSB PDB 5IPY · PDBe 5IPY · UniProt A3SLM3
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