MolNFT v1 · #150513 · protein + DNA

NMR structure of the DNA-bound helix bundle domain from the functional PRN1 primase

6GVU · DNA (5'-D(*CP*TP*GP*TP*GP*CP*TP*CP*A)-3'): “NMR structure of the DNA-bound helix bundle domain from the functional PRN1 primase”. Solution nmr, 1 pocket (best druggability 0.34). MolNFT v1 #150513 on GenesisL1: 3D structure, binding…

PDB: 6GVU
Type: protein + DNA
Length: 124 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA (5'-D(*CP*TP*GP*TP*GP*CP*TP*CP*A)-3'); Functional PRN1 primase
UniProt: Q54324
Pockets: 1 · best druggability 0.34

Structure

solution nmr · 2 distinct chains · 63% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA (5'-D(CPTPGPTPGPCPTPCP*A)-3')	dna	9	—	—
B	Functional PRN1 primase	protein	115	63% helix, 0% strand	Q54324

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	53	0.34	0.78	11	empty

Interfaces

1 interface between chains.

A–B · 775 Å² buried · 12 hydrogen bonds · protein-nucleic

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

6GVU · NMR structure of the DNA-bound helix bundle domain from the functional pRN1 primase · the same entry in another collection · chain A against A, TM-score 1.00

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 Q54324
Elsewhere: RCSB PDB 6GVU · PDBe 6GVU · UniProt Q54324

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