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Symmetric model of CD4- and 17-bound B41 HIV-1 env sosip in complex with small molecule GO52

Analyse Symmetric model of CD4- and 17-bound B41 HIV-1 env sosip in complex with small… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6X5B
Type: protein
Length: 2,487 residues
Chains: 15
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: B3UES2, B3UEZ6, P01730
Ligands: UOV, NAG, MAN, BMA

Structure

electron microscopy · 5 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, D, J	—	protein	353	—	B3UES2
B, E, K	—	protein	149	—	B3UEZ6
L, F, M	—	protein	106	—	—
C, G, N	—	protein	96	—	P01730
H, I, O	—	protein	125	—	—

Ligands and binding sites

UOV · N-(4'-methyl[1,1'-biphenyl]-4-yl)-1-oxa-7-azaspiro[3.5]nonane-7-carboxamide · ligand · 3 copies · chains B, K, E
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 39 copies · chains A, D, J, B, E, K
MAN · alpha-D-mannopyranose · sugar · 6 copies · chains A, D, J
BMA · beta-D-mannopyranose · sugar · 3 copies

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

Compared structures

6X5B · Symmetric model of CD4- and 17-bound B41 HIV-1 Env SOSIP in complex with small molecule… · the same entry in another collection · chain O against O, 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 B3UES2
Every structure of UniProt B3UEZ6
Every structure of UniProt P01730
Elsewhere: RCSB PDB 6X5B · PDBe 6X5B · UniProt B3UES2 · UniProt B3UEZ6 · UniProt P01730

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