MolNFT v1 · #14183 · protein
Human acidic fibroblast growth factor. 141 amino acid form with amino terminal his tag and leu 44 replaced with phe (L44F), leu 73 replaced with val (L73V), val 109 replaced with leu (V109L) and cys 117 replaced with val (C117V).
1M16: “Human acidic fibroblast growth factor. 141 amino acid form with amino terminal his tag and leu 44 replaced…”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.38). MolNFT v1 #14183 on GenesisL1: 3D structure, binding…
- PDB
- 1M16
- Type
- protein
- Length
- 284 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acidic fibroblast growth factor
- UniProt
- P05230
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.38
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Acidic fibroblast growth factor | protein | 142 | 6% helix, 40% strand | P05230 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
- FMT · Formic acid · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 115 | 0.38 | 0.75 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 435 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 1M16 · 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 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 1M16 · PDBe 1M16 · UniProt P05230
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