Research workbench
Crystal structure of tmm from strain HTCC7211 soaked with dms for 20 min
Analyse Crystal structure of tmm from strain HTCC7211 soaked with dms for 20 min in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7D4N
- Type
- protein
- Length
- 886 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flavin-containing monooxygenase fmo
- UniProt
- B6BQB2
- Ligands
- NAP, FAD
- Pockets
- 7 · best druggability 0.88
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flavin-containing monooxygenase fmo | protein | 442 | 33% helix, 21% strand | B6BQB2 |
| B | Flavin-containing monooxygenase fmo | protein | 444 | 32% helix, 21% strand | B6BQB2 |
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
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 595 | 0.88 | 0.94 | 76 | NAP, FAD |
| 2 | 529 | 0.87 | 0.93 | 79 | FAD |
| 3 | 77 | 0.64 | 0.91 | 21 | empty |
| 4 | 106 | 0.50 | 0.82 | 22 | empty |
| 5 | 122 | 0.49 | 0.80 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1716 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 7D4N · Crystal structure of Tmm from strain HTCC7211 soaked with DMS for 20 min · 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 B6BQB2
- Elsewhere: RCSB PDB 7D4N · PDBe 7D4N · UniProt B6BQB2
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