Research workbench
PFKB(MYCOBACTERIUM marinum)
Analyse PFKB(MYCOBACTERIUM marinum) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7FCA
- Type
- protein
- Length
- 1,655 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fructokinase, pfkb
- UniProt
- B2HEF4
- Ligands
- PO4
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 6 distinct chains · 43% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fructokinase, pfkb | protein | 280 | 43% helix, 21% strand | B2HEF4 |
| B | Fructokinase, pfkb | protein | 272 | 43% helix, 21% strand | B2HEF4 |
| C | Fructokinase, pfkb | protein | 273 | 42% helix, 21% strand | B2HEF4 |
| D | Fructokinase, pfkb | protein | 282 | 43% helix, 21% strand | B2HEF4 |
| E | Fructokinase, pfkb | protein | 278 | 43% helix, 21% strand | B2HEF4 |
| F | Fructokinase, pfkb | protein | 270 | 42% helix, 19% strand | B2HEF4 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 5 copies · chains A, B, D, E, F
- GOL · Glycerol · additive · 5 copies · chains A, B, D, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1039 | 0.81 | 0.82 | 85 | empty |
| 2 | 555 | 0.72 | 0.80 | 49 | empty |
| 3 | 505 | 0.67 | 0.78 | 64 | GOL |
| 4 | 89 | 0.66 | 0.91 | 20 | empty |
| 5 | 345 | 0.64 | 0.79 | 43 | GOL |
Interfaces
8 interfaces between chains.
- A–B · 431 Ų buried · 7 hydrogen bonds · protein-protein
- C–E · 410 Ų buried · 12 hydrogen bonds · protein-protein
- D–F · 387 Ų buried · 10 hydrogen bonds · protein-protein
- A–D · 340 Ų buried · 3 hydrogen bonds · protein-protein
- A–C · 338 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 7FCA · PfkB(Mycobacterium marinum) · 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 B2HEF4
- Elsewhere: RCSB PDB 7FCA · PDBe 7FCA · UniProt B2HEF4
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