Research workbench

HLA-B*27:05 presenting an HIV-1 11MER peptide

Analyse HLA-B*27:05 presenting an HIV-1 11MER peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6VPZ
Type: protein
Length: 387 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: O78189, P61769

Structure

x-ray diffraction · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	276	—	O78189
B	—	protein	100	—	P61769
C	—	protein	11	—	—

Ligands and binding sites

GOL · Glycerol · additive · chains A

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

Compared structures

6VPZ · HLA-B*27:05 presenting an HIV-1 11mer peptide · the same entry in another collection · chain A against A, TM-score 1.00
P61769 · AlphaFold monomer V2.0 prediction for beta-2-microglobulin (P61769) · a predicted model of the same protein · chain B against A, TM-score 0.98

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 O78189
Every structure of UniProt P61769
Elsewhere: RCSB PDB 6VPZ · PDBe 6VPZ · UniProt O78189 · UniProt P61769

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