MolNFT v1 · #18790 · protein
Crystal structure of FGF-1, V51N mutant
1PZZ · Heparin-binding growth factor 1: “Crystal structure of FGF-1, V51N mutant”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.41). MolNFT v1 #18790 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1PZZ
- 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 0.41
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Heparin-binding growth factor 1 | protein | 140 | 6% helix, 39% strand | P05230 |
| B | Heparin-binding growth factor 1 | protein | 142 | 8% 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 | 122 | 0.41 | 0.76 | 23 | empty |
| 2 | 55 | 0.40 | 0.81 | 18 | empty |
| 3 | 54 | 0.25 | 0.73 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 439 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
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 1PZZ · PDBe 1PZZ · UniProt P05230
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