5M33: Structural tuning of CD81LEL

Structural tuning of CD81LEL (space group P21). Determined by X-ray diffraction at 1.28 Å resolution. Released 14 Dec 2016.

Method
X-ray diffraction
Resolution
1.28 Å
Organism
Homo sapiens
Chains
2
Atoms
1,650
Mol. weight
22.8 kDa
Released
14 Dec 2016

Explore 5M33 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5M33 contains 12 α-helices and 0 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 6 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix116-13621
α-helix141-15414
α-helix163-1653
α-helix166-1716
α-helix181-1855
α-helix190-19910
Chain B: 6 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix113-1153
α-helix116-13520
α-helix143-15412
α-helix163-1719
α-helix179-1835
α-helix190-19910

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
CD81 antigenA, Bprotein101Homo sapiensP60033 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>5M33_1 CD81 antigen (chains A, B)
ETGFVNKDQIAKDVKQFYDQALQQAVVDDDANNAKAVVKTFHETLDCCGSSTLTALTTSV
LKNNLCPSGSNIISNLFKEDCHQKIDDLFSGKGTKHHHHHH

Primary citation

Mechanism of Structural Tuning of the Hepatitis C Virus Human Cellular Receptor CD81 Large Extracellular Loop. Cunha, E.S., Sfriso, P., Rojas, A.L. et al. Structure (2017) 25:53-65. DOI 10.1016/j.str.2016.11.003 · PubMed

Other PDB entries of the same protein (UniProt P60033 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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