MolNFT v1 · #63761 · protein
Crystal structure of C83V mutant of human acidic fibroblast growth factor
3FJJ · Heparin-binding growth factor 1: “Crystal structure of C83V mutant of human acidic fibroblast growth factor”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.40). MolNFT v1 #63761 on GenesisL1: 3D structure…
- PDB
- 3FJJ
- Type
- protein
- Length
- 282 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heparin-binding growth factor 1
- UniProt
- P05230
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Heparin-binding growth factor 1 | protein | 141 | 6% helix, 37% strand | P05230 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 112 | 0.40 | 0.76 | 22 | empty |
| 2 | 56 | 0.40 | 0.81 | 17 | empty |
| 3 | 54 | 0.30 | 0.76 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 421 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 3FJJ · Crystal structure of C83V mutant of Human acidic fibroblast growth factor · the same entry in another collection · chain A against A, TM-score 1.00
- P05230 · AlphaFold monomer V2.0 prediction for fibroblast growth factor 1 (P05230) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P05230
- Elsewhere: RCSB PDB 3FJJ · PDBe 3FJJ · UniProt P05230
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