MolNFT v1 · #162925 · protein
Dipeptide gly-pro binds to a glycolytic enzyme fructose bisphosphate aldolase
6RNG: “Dipeptide gly-pro binds to a glycolytic enzyme fructose bisphosphate aldolase”. X-ray diffraction, 1 ligand (SO4). MolNFT v1 #162925 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6RNG
- Type
- protein
- Length
- 1,348 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9SJQ9
- Ligands
- SO4
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, F | — | protein | 337 | — | Q9SJQ9 |
| B | — | protein | 336 | — | Q9SJQ9 |
| G | — | protein | 338 | — | Q9SJQ9 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 13 copies · chains A, B, F, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6RNG · Dipeptide Gly-Pro binds to a glycolytic enzyme fructose bisphosphate aldolase · the same entry in another collection · chain G against G, TM-score 1.00
- Q9SJQ9 · AlphaFold monomer V2.0 prediction for fructose-bisphosphate aldolase 6, cytosolic (Q9SJQ9) · a predicted model of the same protein · 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 Q9SJQ9
- Elsewhere: RCSB PDB 6RNG · PDBe 6RNG · UniProt Q9SJQ9
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