Research workbench
MSMEG_3358 F420 reductase
Analyse MSMEG_3358 F420 reductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3H96
- Type
- protein
- Length
- 550 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- F420-H2 dependent reductase a
- UniProt
- A0QXM5
- Pockets
- 5 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | F420-H2 dependent reductase a | protein | 137 | 35% helix, 31% strand | A0QXM5 |
| C, D | F420-H2 dependent reductase a | protein | 138 | 36% helix, 31% strand | A0QXM5 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 517 | 0.65 | 0.77 | 61 | empty |
| 2 | 476 | 0.64 | 0.77 | 62 | empty |
| 3 | 123 | 0.46 | 0.77 | 18 | empty |
| 4 | 135 | 0.45 | 0.76 | 19 | empty |
| 5 | 99 | 0.34 | 0.73 | 21 | empty |
Interfaces
4 interfaces between chains.
- A–D · 367 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 361 Ų buried · 1 hydrogen bond · protein-protein
- A–B · 353 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 347 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 3H96 · Msmeg_3358 F420 Reductase · 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 A0QXM5
- Elsewhere: RCSB PDB 3H96 · PDBe 3H96 · UniProt A0QXM5
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