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Artificial HIV fusion inhibitor AP2 fused to the C-terminus of GP41 nhr

Analyse Artificial HIV fusion inhibitor AP2 fused to the C-terminus of GP41 nhr in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5CN0
Type: protein
Length: 70 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Envelope GLYCOPROTEIN,AP2
UniProt: Q1HMR5
Ligands: MG

Structure

x-ray diffraction · 1 distinct chain · 84% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Envelope GLYCOPROTEIN,AP2	protein	70	84% helix, 0% strand	Q1HMR5

Ligands and binding sites

MG · Magnesium ion · metal · chains A
PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A

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

Compared structures

5CN0 · Artificial HIV fusion inhibitor AP2 fused to the C-terminus of gp41 NHR · 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 Q1HMR5
Elsewhere: RCSB PDB 5CN0 · PDBe 5CN0 · UniProt Q1HMR5

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