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AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta' (Q18CF3)

Analyse AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta'… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: Q18CF3
Type: protein
Length: 1,161 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x0D671490EE06E75975e90D7F99F73B20BE618744
Molecule: DNA-directed RNA polymerase subunit beta'
UniProt: Q18CF3
Pockets: 15 · best druggability 0.75

Structure

1 distinct chain · 45% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA-directed RNA polymerase subunit beta'	protein	1161	45% helix, 16% strand	Q18CF3

Pockets

15 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	835	0.75	0.79	76	empty
2	661	0.71	0.78	39	empty
3	894	0.70	0.75	57	empty
4	589	0.67	0.77	63	empty
5	62	0.58	0.89	18	empty

Compared structures

7L7B · Clostridioides difficile rnap with fidaxomicin · an experimental structure of the same protein · chain A against D, TM-score 0.96
7L7B · Clostridioides difficile RNAP with fidaxomicin · an experimental structure of the same protein · chain A against D, TM-score 0.96

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 Q18CF3
Elsewhere: UniProt Q18CF3 · AlphaFold DB Q18CF3

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