Research workbench

AlphaFold monomer V2.0 prediction for translocation and assembly module subunit tamb (P39321)

Analyse AlphaFold monomer V2.0 prediction for translocation and assembly module subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P39321
Type: protein
Length: 1,259 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x6DAA77C4263E74E745cA9c4D8E291e57e8991Cf5
Molecule: Translocation and assembly module subunit tamb
UniProt: P39321
Pockets: 6 · best druggability 0.76

Structure

1 distinct chain · 10% helix, 63% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Translocation and assembly module subunit tamb	protein	1259	10% helix, 63% strand	P39321

Pockets

6 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	670	0.76	0.82	75	empty
2	886	0.71	0.74	66	empty
3	115	0.41	0.76	17	empty
4	63	0.40	0.80	19	empty
5	116	0.35	0.72	22	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

5VTG · The structure of TAMB963-1138 from escherichia COLI reveals a novel hydrophobic beta-taco… · an experimental structure of the same protein · chain A against A, TM-score 0.10
5VTG · The structure of TamB963-1138 from Escherichia coli reveals a novel hydrophobic Beta-taco… · 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 P39321
Elsewhere: UniProt P39321 · AlphaFold DB P39321

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.