MolNFT v1 · #6555 · protein
Refinement of the structure of human basic fibroblast growth factor at 1.6 ångströms resolution and analysis of presumed heparin binding sites by selenate substitution
1FGA: “Refinement of the structure of human basic fibroblast growth factor at 1.6 ångströms resolution and analysis…”. X-ray diffraction, 1 ligand (SE4). MolNFT v1 #6555 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1FGA
- Type
- protein
- Length
- 124 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Basic fibroblast growth factor
- UniProt
- P09038
- Ligands
- SE4
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Basic fibroblast growth factor | protein | 124 | 7% helix, 37% strand | P09038 |
Ligands and binding sites
- SE4 · Selenate ion · ion · 2 copies · chains A
- BME · Beta-mercaptoethanol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 2 covalent (additive adduct).
Compared structures
- 1FGA · Refinement of the structure of human basic fibroblast growth factor at 1.6 ångströms… · 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 1FGA · PDBe 1FGA · UniProt P09038
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