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AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit beta' (Q31N15)

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: Q31N15
Type: protein
Length: 1,318 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xf4ED13986579E8e227b3ED6c02276c648754EC27
Molecule: DNA-directed RNA polymerase subunit beta'
UniProt: Q31N15
Pockets: 11 · best druggability 0.81

Structure

1 distinct chain · 25% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA-directed RNA polymerase subunit beta'	protein	1318	25% helix, 31% strand	Q31N15

Pockets

11 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	1076	0.81	0.82	117	empty
2	832	0.77	0.81	84	empty
3	192	0.48	0.75	27	empty
4	86	0.45	0.81	16	empty
5	148	0.42	0.75	19	empty

Compared structures

8SYI · Cyanobacterial RNAP-EC · an experimental structure of the same protein · chain A against Z, TM-score 0.72
8URW · Cyanobacterial RNA polymerase elongation complex with NusG and CTP · an experimental structure of the same protein · chain A against Z, TM-score 0.62
8H02 · Crystal structure of Synechococcus elongatus PCC 7942 RNA polymerase SI3-tail · an experimental structure of the same protein · chain A against A, TM-score 0.06

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 Q31N15
Elsewhere: UniProt Q31N15 · AlphaFold DB Q31N15

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