MolNFT v1 · #41312 · protein
Fructose-1,6-BISPHOSPHATASE(D-fructose-1,6-bisphosphate -1-phosphohydrolase) (E.C.3.1.3.11) complexed with a dual binding AMP site inhibitor
2JJK: “Fructose-1,6-BISPHOSPHATASE(D-fructose-1,6-bisphosphate -1-phosphohydrolase) (E.C.3.1.3.11) complexed with a…”. X-ray diffraction. MolNFT v1 #41312 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2JJK
- Type
- protein
- Length
- 1,271 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P09467
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 319 | — | P09467 |
| B, D | — | protein | 317 | — | P09467 |
| C | — | protein | 318 | — | P09467 |
Compared structures
- 2JJK · Fructose-1,6-BISPHOSPHATASE(D-fructose-1,6-bisphosphate -1- phosphohydrolase)… · the same entry in another collection · chain D against D, TM-score 1.00
- P09467 · AlphaFold monomer V2.0 prediction for fructose-1,6-bisphosphatase 1 (P09467) · a predicted model of the same protein · chain D against A, TM-score 0.97
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 P09467
- Elsewhere: RCSB PDB 2JJK · PDBe 2JJK · UniProt P09467
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