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MolNFT v1 · #165603 · protein

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

6U0L: “Asymmetrically open conformational state (class I) of HIV-1 env trimer BG505 SOSIP.664 in complex with SCD4…”. Electron microscopy, 3 ligands (NAG, MAN, BMA). MolNFT v1 #165603 on GenesisL1: 3D structure, binding sites and pockets…

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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