MolNFT v1 · #82303 · protein

HIV-GP41 fusion inhibitor sifuvirtide

3VIE · Envelope glycoprotein GP160: “HIV-GP41 fusion inhibitor sifuvirtide”. X-ray diffraction, 1 ligand (ACE). MolNFT v1 #82303 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3VIE
Type: protein
Length: 215 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Envelope glycoprotein GP160; Sifuvirtide
UniProt: Q9YP39
Ligands: ACE

Structure

x-ray diffraction · 3 distinct chains · 94% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Envelope glycoprotein GP160	protein	35	94% helix, 0% strand	Q9YP39
C, E	Envelope glycoprotein GP160	protein	36	94% helix, 0% strand	Q9YP39
B, D, F	Sifuvirtide	protein	36	94% helix, 0% strand	—

Ligands and binding sites

ACE · Acetyl group · ligand · 6 copies · chains A, C, B, D, E, F

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

Interfaces

9 interfaces between chains.

A–F · 794 Å² buried · 9 hydrogen bonds · protein-protein
E–D · 792 Å² buried · 12 hydrogen bonds · protein-protein
C–B · 784 Å² buried · 5 hydrogen bonds · protein-protein
C–D · 716 Å² buried · 6 hydrogen bonds · protein-protein
A–B · 696 Å² buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 covalent (covalent ligand).

Compared structures

3VIE · HIV-gp41 fusion inhibitor Sifuvirtide · 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 Q9YP39
Elsewhere: RCSB PDB 3VIE · PDBe 3VIE · UniProt Q9YP39

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