MolNFT v1 · #12082 · protein
Human acidic fibroblast growth factor. 141 amino acid form with amino terminal his tag with HIS93 replaced by gly (H93G).
1K5U: “Human acidic fibroblast growth factor. 141 amino acid form with amino terminal his tag with HIS93 replaced by…”. X-ray diffraction, 1 ligand (SO4), 2 pockets (best druggability 0.58). MolNFT v1 #12082 on GenesisL1: 3D structure…
- PDB
- 1K5U
- Type
- protein
- Length
- 386 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acidic fibroblast growth factor
- UniProt
- P05230
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 12% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Acidic fibroblast growth factor | protein | 129 | 12% helix, 40% strand | P05230 |
| B | Acidic fibroblast growth factor | protein | 128 | 12% helix, 40% strand | P05230 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 361 | 0.58 | 0.76 | 46 | empty |
| 2 | 50 | 0.36 | 0.80 | 14 | empty |
Interfaces
2 interfaces between chains.
- A–C · 284 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 218 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1K5U · Human acidic fibroblast growth factor. 141 amino acid form with amino terminal His tag… · 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 C 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 P05230
- Elsewhere: RCSB PDB 1K5U · PDBe 1K5U · UniProt P05230
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