MolNFT v1 · #153760 · protein

Crystal structures of phage nrs-1 N300-dntps-MG2+ complex provide molecular mechanisms for substrate specificity

6JOQ · Primase: “Crystal structures of phage nrs-1 N300-dntps-MG2+ complex provide molecular mechanisms for substrate…”. X-ray diffraction, 2 ligands (DGT, MG), 1 pocket (best druggability 0.49). MolNFT v1 #153760 on GenesisL1: 3D…

PDB: 6JOQ
Type: protein
Length: 280 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Primase
UniProt: M5AAG8
Ligands: DGT, MG
Pockets: 1 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Primase	protein	280	32% helix, 21% strand	M5AAG8

Ligands and binding sites

DGT · 2'-deoxyguanosine-5'-triphosphate · ligand · chains A
MG · Magnesium ion · metal · 2 copies · chains A

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

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	139	0.49	0.79	23	DGT, MG

Compared structures

6JOQ · Crystal structures of phage NrS-1 N300-dNTPs-Mg2+ complex provide molecular mechanisms… · 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 M5AAG8
Elsewhere: RCSB PDB 6JOQ · PDBe 6JOQ · UniProt M5AAG8

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