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Structure of deep-sea phage nrs-1 primase-polymerase N300 in complex with magnesium and pyrophosphate

Analyse Structure of deep-sea phage nrs-1 primase-polymerase N300 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7RR4
Type: protein
Length: 273 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Primase
UniProt: M5AAG8
Ligands: PPV, MG
Pockets: 1 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Primase	protein	273	32% helix, 22% strand	M5AAG8

Ligands and binding sites

PPV · Pyrophosphate · 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	104	0.43	0.78	19	MG, PPV

Compared structures

7RR4 · Structure of Deep-Sea Phage NrS-1 Primase-Polymerase N300 in complex with magnesium and… · 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 7RR4 · PDBe 7RR4 · UniProt M5AAG8

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