Research workbench

AlphaFold monomer V2.0 prediction for ferric uptake regulation protein (P0A9A9)

Analyse AlphaFold monomer V2.0 prediction for ferric uptake regulation protein (P0A9A9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P0A9A9
Type: protein
Length: 148 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xEa58c7534E5701aA8370E0fAEb19b7e14653e69c
Molecule: Ferric uptake regulation protein
UniProt: P0A9A9
Pockets: 3 · best druggability 0.44

Structure

1 distinct chain · 38% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ferric uptake regulation protein	protein	148	38% helix, 17% strand	P0A9A9

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	190	0.44	0.74	29	empty
2	51	0.27	0.75	16	empty
3	50	0.26	0.74	10	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

8J6W · Full length crystal structure of Escherichia coli Fur · an experimental structure of the same protein · chain A against A, TM-score 0.75
2FU4 · Crystal Structure of the DNA binding domain of E.coli FUR (Ferric Uptake Regulator) · an experimental structure of the same protein · chain A against B, TM-score 0.54
2FU4 · Crystal structure of the DNA binding domain of E.COLI fur (ferric uptake regulator) · an experimental structure of the same protein · chain A against B, TM-score 0.54

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 P0A9A9
Elsewhere: UniProt P0A9A9 · AlphaFold DB P0A9A9

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