MolNFT v1 · #131265 · protein
Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed with the allosteric inhibitor 1-(4-bromo-5-chlorothiophen-2-YL)SULFONYL-3-(5-bromo-1,3-thiazol-2- YL)UREA
5Q04: “Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed…”. X-ray diffraction, 1 ligand (95P). MolNFT v1 #131265 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5Q04
- Type
- protein
- Length
- 2,540 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q2TU34
- Ligands
- 95P
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E | — | protein | 319 | — | Q2TU34 |
| B, C, D, F, G, H | — | protein | 317 | — | Q2TU34 |
Ligands and binding sites
- 95P · 4-bromo-N-[(5-bromo-1,3-thiazol-2-yl)carbamoyl]-5-chlorothiophene-2-sulfonamide · ligand · 8 copies · chains A, C, B, D, E, G, F, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5Q04 · Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase… · 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 Q2TU34
- Elsewhere: RCSB PDB 5Q04 · PDBe 5Q04 · UniProt Q2TU34
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