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Crystal structure of the bacillus subtilis dnag RNA polymerase domain, natural degradation of full length dnag

Analyse Crystal structure of the bacillus subtilis dnag RNA polymerase domain, natural… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5GUJ
Type: protein
Length: 324 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA primase
EC: 2.7.7.-
UniProt: P05096
Pockets: 1 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA primase (EC 2.7.7.-)	protein	324	51% helix, 15% strand	P05096

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	182	0.54	0.79	35	empty

Compared structures

5GUJ · Crystal structure of the Bacillus subtilis DnaG RNA Polymerase Domain, natural… · the same entry in another collection · chain A against A, TM-score 1.00
P05096 · AlphaFold monomer V2.0 prediction for DNA primase (P05096) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P05096
Elsewhere: RCSB PDB 5GUJ · PDBe 5GUJ · UniProt P05096

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