Research workbench
Crystal structure of leishmania major fructose-1,6-bisphosphatase in holo form.
Analyse Crystal structure of leishmania major fructose-1,6-bisphosphatase in holo form. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OEY
- Type
- protein
- Length
- 1,271 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fbp protein
- EC
- 3.1.3.11
- UniProt
- O97193
- Ligands
- MN, K, PO4
- Pockets
- 14 · best druggability 0.83
Structure
x-ray diffraction · 4 distinct chains · 38% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fbp protein (EC 3.1.3.11) | protein | 325 | 38% helix, 25% strand | O97193 |
| B | Fbp protein (EC 3.1.3.11) | protein | 319 | 38% helix, 25% strand | O97193 |
| C | Fbp protein (EC 3.1.3.11) | protein | 326 | 37% helix, 25% strand | O97193 |
| D | Fbp protein (EC 3.1.3.11) | protein | 301 | 38% helix, 26% strand | O97193 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 8 copies · chains A, B, C, D
- K · Potassium ion · metal · 4 copies · chains A, B, C, D
- PO4 · Phosphate ion · ion · 4 copies · chains A, B, C, D
- CIT · Citric acid · additive · 2 copies · chains A, C, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 241 | 0.83 | 0.96 | 40 | empty |
| 2 | 67 | 0.72 | 0.97 | 23 | empty |
| 3 | 375 | 0.63 | 0.79 | 45 | PO4, K |
| 4 | 319 | 0.63 | 0.80 | 42 | PO4, K |
| 5 | 208 | 0.56 | 0.79 | 37 | empty |
Interfaces
6 interfaces between chains.
- A–B · 2270 Ų buried · 38 hydrogen bonds · protein-protein
- C–D · 2232 Ų buried · 42 hydrogen bonds · protein-protein
- A–D · 1360 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 1242 Ų buried · 13 hydrogen bonds · protein-protein
- B–D · 62 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 5OEY · Crystal structure of Leishmania major fructose-1,6-bisphosphatase in holo form. · the same entry in another collection · chain B against B, 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 O97193
- Elsewhere: RCSB PDB 5OEY · PDBe 5OEY · UniProt O97193
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