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Asymmetrically open conformational state (class I) of HIV-1 env trimer BG505 SOSIP.664 in complex with SCD4 and E51 Fab

Analyse Asymmetrically open conformational state (class I) of HIV-1 env trimer BG505… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6U0L
Type
protein
Length
2,501 residues
Chains
15
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
Q2N0S6, P01730
Ligands
NAG, MAN, BMA

Structure

electron microscopy · 9 distinct chains.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein365—Q2N0S6
B—protein367—Q2N0S6
C—protein365—Q2N0S6
D, E, F—protein97—P01730
H, I, P—protein132——
J, L, Q—protein110——
X—protein133—Q2N0S6
Y—protein133—Q2N0S6
Z—protein121—Q2N0S6

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 35 copies · chains A, H, B, I, C, P, Z, X
  • MAN · alpha-D-mannopyranose · sugar · 8 copies · chains A, B, C
  • BMA · beta-D-mannopyranose · sugar · 3 copies

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

Compared structures

  • 6U0L · Asymmetrically open conformational state (Class I) of HIV-1 Env trimer BG505 SOSIP.664 in… · the same entry in another collection · chain Z against Z, TM-score 1.00

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