Research workbench

Crystal structures of feline immunodeficiency virus dutp pyrophosphatase and its nucleotide complexes in three crystal forms.

Analyse Crystal structures of feline immunodeficiency virus dutp pyrophosphatase and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1F7O
Type: protein
Length: 347 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pol polyprotein
EC: 3.6.1.23
UniProt: P16088
Pockets: 3 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 3% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Pol polyprotein (EC 3.6.1.23)	protein	116	3% helix, 45% strand	P16088
C	Pol polyprotein (EC 3.6.1.23)	protein	115	3% helix, 50% strand	P16088

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	450	0.79	0.87	86	empty
2	118	0.45	0.77	19	empty
3	97	0.38	0.75	22	empty

Interfaces

3 interfaces between chains.

A–C · 1442 Å² buried · 17 hydrogen bonds · protein-protein
B–C · 1401 Å² buried · 18 hydrogen bonds · protein-protein
A–B · 1286 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

1F7O · Crystal structures of feline immunodeficiency virus dutp pyrophosphatase and its… · the same entry in another collection · chain B against B, 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 P16088
Elsewhere: RCSB PDB 1F7O · PDBe 1F7O · UniProt P16088

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.