MolNFT v1 · #82658 · protein

Novel HIV fusion inhibitor

3VTQ · Envelope glycoprotein GP160: “Novel HIV fusion inhibitor”. X-ray diffraction, 2 ligands (ACE, NH2). MolNFT v1 #82658 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3VTQ
Type: protein
Length: 219 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Envelope glycoprotein GP160; Fusion inhibitor mt-sifuvirtide
UniProt: Q9YP39
Ligands: ACE, NH2

Structure

x-ray diffraction · 2 distinct chains · 93% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
E, A, B	Envelope glycoprotein GP160	protein	36	94% helix, 0% strand	Q9YP39
D, C, F	Fusion inhibitor mt-sifuvirtide	protein	37	92% helix, 0% strand	—

Ligands and binding sites

ACE · Acetyl group · ligand · 6 copies · chains E, B, D, A, C, F
NH2 · Amino group · ion · chains F

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

Interfaces

9 interfaces between chains.

E–C · 841 Å² buried · 11 hydrogen bonds · protein-protein
A–F · 832 Å² buried · 7 hydrogen bonds · protein-protein
B–D · 824 Å² buried · 8 hydrogen bonds · protein-protein
A–B · 713 Å² buried · 5 hydrogen bonds · protein-protein
E–A · 683 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

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

Compared structures

3VTQ · Novel HIV fusion inhibitor · the same entry in another collection · chain E against E, 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 3VTQ · PDBe 3VTQ · UniProt Q9YP39

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