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AlphaFold monomer V2.0 prediction for fibroblast growth factor receptor 2 (P21803)

Analyse AlphaFold monomer V2.0 prediction for fibroblast growth factor receptor 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P21803
Type: protein
Length: 821 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x429aA010A80A47FF4a2777bB34A2bba144d19df2
Molecule: Fibroblast growth factor receptor 2
UniProt: P21803
Pockets: 6 · best druggability 0.75

Structure

1 distinct chain · 21% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fibroblast growth factor receptor 2	protein	821	21% helix, 24% strand	P21803

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	471	0.75	0.83	61	empty
2	310	0.73	0.86	39	empty
3	174	0.50	0.77	24	empty
4	262	0.49	0.74	30	empty
5	56	0.37	0.80	15	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

4HWU · Crystal structure of the Ig-C2 type 1 domain from mouse Fibroblast growth factor receptor… · an experimental structure of the same protein · chain A against A, TM-score 0.10
4HWU · Crystal structure of the ig-C2 type 1 domain from mouse fibroblast growth factor receptor… · an experimental structure of the same protein · chain A against A, TM-score 0.10

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 P21803
Elsewhere: UniProt P21803 · AlphaFold DB P21803

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