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3.5 ångström crystal structure of a fully and natively glycosylated BG505 SOSIP.664 HIV-1 env trimer in complex with the broadly neutralizing antibodies ioma and 10-1074

Analyse 3.5 ångström crystal structure of a fully and natively glycosylated BG505… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5T3Z
Type: protein
Length: 1,456 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: Q2N0S6
Ligands: NAG, MAN, BMA, FUC, GAL

Structure

x-ray diffraction · 6 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	—	protein	126	—	Q2N0S6
G	—	protein	450	—	Q2N0S6
H	—	protein	230	—	—
L	—	protein	211	—	—
D	—	protein	229	—	—
E	—	protein	210	—	—

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 42 copies · chains B, G, L, D, E, H
MAN · alpha-D-mannopyranose · sugar · 27 copies · chains L, D, G, E, H
BMA · beta-D-mannopyranose · sugar · 12 copies · chains D, H
FUC · alpha-L-fucopyranose · sugar · 4 copies · chains B, G, D
GAL · beta-D-galactopyranose · sugar · 4 copies

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

Compared structures

5T3Z · 3.5 Angstrom Crystal Structure of a Fully and Natively Glycosylated BG505 SOSIP.664 HIV-1… · the same entry in another collection · chain B against B, 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 Q2N0S6
Elsewhere: RCSB PDB 5T3Z · PDBe 5T3Z · UniProt Q2N0S6

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