MolNFT v1 · #63179 · protein

Crystal structure of FGF20 dimer

3F1R · Fibroblast growth factor 20: “Crystal structure of FGF20 dimer”. X-ray diffraction, 1 ligand (SO4), 3 pockets (best druggability 0.55). MolNFT v1 #63179 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3F1R
Type: protein
Length: 314 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fibroblast growth factor 20
UniProt: Q9NP95
Ligands: SO4
Pockets: 3 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Fibroblast growth factor 20	protein	157	15% helix, 40% strand	Q9NP95

Ligands and binding sites

SO4 · Sulfate ion · ion · 6 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	126	0.55	0.83	24	empty
2	157	0.51	0.79	24	empty
3	52	0.30	0.76	12	empty

Interfaces

1 interface between chains.

A–B · 1126 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

3F1R · Crystal structure of FGF20 dimer · the same entry in another collection · chain A against A, TM-score 1.00
Q9NP95 · AlphaFold monomer V2.0 prediction for fibroblast growth factor 20 (Q9NP95) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q9NP95
Elsewhere: RCSB PDB 3F1R · PDBe 3F1R · UniProt Q9NP95

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