MolNFT v1 · #91626 · protein

Fiv protease complexed with an inhibitor lp-130

4FIV · Feline immunodeficiency virus protease: “Fiv protease complexed with an inhibitor lp-130”. X-ray diffraction, 1 ligand (LP1), 2 pockets (best druggability 0.54). MolNFT v1 #91626 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 4FIV
Type: protein
Length: 113 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Feline immunodeficiency virus protease
EC: 3.4.23.16
UniProt: P16088
Ligands: LP1
Pockets: 2 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Feline immunodeficiency virus protease (EC 3.4.23.16)	protein	113	8% helix, 44% strand	P16088

Ligands and binding sites

LP1 · 4-[2-(2-acetylamino-3-naphtalen-1-yl-propionylamino)-4-methyl-pentanoylamino]-3-hydroxy-6-methyl-heptanoic acid [1-(1-carbamoyl-2-naphthalen-1-yl-ethylcarbamoyl)-propyl]-amide · ligand · chains A

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

Pockets

2 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	203	0.54	0.78	22	empty
2	108	0.37	0.74	21	empty

Compared structures

4FIV · Fiv protease complexed with an inhibitor lp-130 · 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 P16088
Elsewhere: RCSB PDB 4FIV · PDBe 4FIV · UniProt P16088

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