Research workbench

Cryo-EM structure of bacillus subtilis RNA polymerase elongation complex

Analyse Cryo-EM structure of bacillus subtilis RNA polymerase elongation complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6WVJ
Type: protein + DNA + RNA
Length: 2,839 residues
Chains: 8
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P20429, A0A2J0WBQ0, A0A063XB23, A0A063XI46
Ligands: ZN, MG

Structure

electron microscopy · 7 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	—	protein	224	—	P20429
C	—	protein	1117	—	A0A2J0WBQ0
D	—	protein	1176	—	A0A063XB23
F	—	protein	61	—	A0A063XI46
T	—	dna	19	—	—
R	—	rna	8	—	—
N	—	dna	10	—	—

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains D
MG · Magnesium ion · metal · chains D, R

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

6WVJ · Cryo-EM structure of Bacillus subtilis RNA Polymerase elongation complex · the same entry in another collection · chain N against N, TM-score 1.00
P20429 · AlphaFold monomer V2.0 prediction for DNA-directed RNA polymerase subunit alpha (P20429) · a predicted model of the same protein · chain A against A, TM-score 0.92

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 P20429
Every structure of UniProt A0A2J0WBQ0
Every structure of UniProt A0A063XB23
Every structure of UniProt A0A063XI46
Elsewhere: RCSB PDB 6WVJ · PDBe 6WVJ · UniProt P20429 · UniProt A0A2J0WBQ0 · UniProt A0A063XB23 · UniProt A0A063XI46

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