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RPB5 from S.cerevisiae

Analyse RPB5 from S.cerevisiae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1DZF
Type: protein
Length: 211 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.9
Source: SACCHAROMYCES CEREVISIAE
Molecule: DNA-directed RNA polymerases I, II, and III subunit rpabc 1
EC: 2.7.7.6
UniProt: P20434
Pockets: 3 · best druggability 0.52

Structure

x-ray diffraction · resolution 1.9 · 1 distinct chain · 39% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA-directed RNA polymerases I, II, and III subunit rpabc 1 (EC 2.7.7.6)	protein	211	39% helix, 21% strand	P20434

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	138	0.52	0.80	25	empty
2	150	0.48	0.77	24	empty
3	59	0.29	0.74	11	empty

Compared structures

1DZF · RPB5 from S.CEREVISIAE · the same entry in another collection · chain A against A, TM-score 1.00
P20434 · AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerases I, II, and III subunit… · a predicted model of the same protein · chain A against A, TM-score 0.94

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 P20434
Elsewhere: RCSB PDB 1DZF · PDBe 1DZF · UniProt P20434

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