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Structure of the P2 polymerase inside in vitro assembled bacteriophage PHI6 polymerase complex

Analyse Structure of the P2 polymerase inside in vitro assembled bacteriophage PHI6… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5FJ6
Type: protein
Length: 664 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RNA-directed RNA polymerase
UniProt: P11124
Ligands: MN
Pockets: 8 · best druggability 0.83

Structure

electron microscopy · 1 distinct chain · 42% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RNA-directed RNA polymerase	protein	664	42% helix, 10% strand	P11124

Ligands and binding sites

MN · Manganese (II) ion · metal · chains A

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

Pockets

8 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	233	0.83	0.95	37	empty
2	539	0.81	0.87	70	empty
3	364	0.79	0.89	59	empty
4	117	0.79	0.97	32	empty
5	203	0.70	0.87	33	empty

Compared structures

5FJ6 · Structure of the P2 polymerase inside in vitro assembled bacteriophage phi6 polymerase… · 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 P11124
Elsewhere: RCSB PDB 5FJ6 · PDBe 5FJ6 · UniProt P11124

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