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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: 1F7N
Type: protein
Length: 234 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Pol polyprotein
EC: 3.6.1.23
UniProt: P16088
Ligands: UMP, MG
Pockets: 2 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 3% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Pol polyprotein (EC 3.6.1.23)	protein	117	3% helix, 42% strand	P16088

Ligands and binding sites

UMP · 2'-deoxyuridine 5'-monophosphate · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 3 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	163	0.49	0.77	24	empty
2	50	0.26	0.73	13	empty

Interfaces

1 interface between chains.

A–B · 491 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

1F7N · Crystal structures of feline immunodeficiency virus dutp pyrophosphatase and its… · the same entry in another collection · chain A against A, TM-score 1.00

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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 1F7N · PDBe 1F7N · UniProt P16088

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