Research workbench
Crystal structure of tmm from strain HTCC7211 soaked with dms for 5 min
Analyse Crystal structure of tmm from strain HTCC7211 soaked with dms for 5 min in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7D4M
- 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
- 8 · best druggability 0.88
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Flavin-containing monooxygenase fmo | protein | 444 | 33% helix, 21% strand | B6BQB2 |
| B | Flavin-containing monooxygenase fmo | protein | 442 | 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
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 598 | 0.88 | 0.94 | 81 | NAP, FAD |
| 2 | 607 | 0.88 | 0.93 | 92 | NAP, FAD |
| 3 | 88 | 0.60 | 0.87 | 22 | empty |
| 4 | 107 | 0.51 | 0.82 | 21 | empty |
| 5 | 126 | 0.51 | 0.81 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 1669 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 7D4M · Crystal structure of Tmm from strain HTCC7211 soaked with DMS for 5 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 7D4M · PDBe 7D4M · UniProt B6BQB2
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