MolNFT v1 · #129259 · protein
Crystal structure of leishmania major fructose-1,6-bisphosphatase in holo form.
5OEY: “Crystal structure of leishmania major fructose-1,6-bisphosphatase in holo form.”. X-ray diffraction, 3 ligands (MN, K, PO4). MolNFT v1 #129259 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5OEY
- Type
- protein
- Length
- 1,271 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- O97193
- Ligands
- MN, K, PO4
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 325 | — | O97193 |
| B | — | protein | 319 | — | O97193 |
| C | — | protein | 326 | — | O97193 |
| D | — | protein | 301 | — | 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.
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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