Research workbench
Crystal structure analysis of FGF2-disaccharide (S9I2) complex
Analyse Crystal structure analysis of FGF2-disaccharide (S9I2) complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4OEG
- Type
- protein
- Length
- 124 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fibroblast growth factor 2
- UniProt
- P09038
- Ligands
- IDY, SUS
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fibroblast growth factor 2 | protein | 124 | 10% helix, 43% strand | P09038 |
Ligands and binding sites
- IDY · 1-O-methyl-2-O-sulfo-alpha-L-idopyranuronic acid · ligand · chains A
- SUS · 2-deoxy-3,6-di-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4OEG · Crystal Structure Analysis of FGF2-Disaccharide (S9I2) complex · the same entry in another collection · chain A against A, TM-score 1.00
- P09038 · AlphaFold monomer V2.0 prediction for fibroblast growth factor 2 (P09038) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P09038
- Elsewhere: RCSB PDB 4OEG · PDBe 4OEG · UniProt P09038
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