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AlphaFold monomer V2.0 prediction for natural resistance-associated macrophage protein 1 (P49279)

Analyse AlphaFold monomer V2.0 prediction for natural resistance-associated macrophage… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P49279
Type: protein
Length: 550 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xf1770e5260EEBa91B7A9E674F368eD787DE8992D
Molecule: Natural resistance-associated macrophage protein 1
UniProt: P49279
Pockets: 6 · best druggability 0.62

Structure

1 distinct chain · 74% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Natural resistance-associated macrophage protein 1	protein	550	74% helix, 1% strand	P49279

Pockets

6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	437	0.62	0.75	36	empty
2	294	0.57	0.77	44	empty
3	290	0.56	0.76	27	empty
4	288	0.54	0.76	36	empty
5	142	0.50	0.78	21	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

9F6P · Human NRAMP1 (SLC11A1) in complex with manganese, towards the inward-open state · an experimental structure of the same protein · chain A against A, TM-score 0.85
9F6Q · Human NRAMP1 (SLC11A1) in an occluded state · an experimental structure of the same protein · chain A against A, TM-score 0.83

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 P49279
Elsewhere: UniProt P49279 · AlphaFold DB P49279

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