1CM9: Viral macrophage inflammatory protein-II

Crystal structure of viral macrophage inflammatory protein-II. Determined by X-ray diffraction at 2.1 Å resolution. Released 24 Jun 1999.

Method
X-ray diffraction
Resolution
2.1 Å
Organism
Human herpesvirus 8
Chains
2
Atoms
1,064
Mol. weight
16.93 kDa
Released
24 Jun 1999

Explore 1CM9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1CM9 contains 12 α-helices and 10 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.

Chains A and B: 6 helices, 5 β-strands

ElementResiduesLengthSheet
β-strand12-1431
α-helix22-243
α-helix25-273
β-strand28-3362
α-helix34-352
β-strand43-4752
β-strand52-5542
α-helix60-689
α-helix701
β-strand7112
α-helix721

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein (viral macrophage inflammatory protein-II)A, Bprotein74Human herpesvirus 8Q98157 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1CM9_1 PROTEIN (VIRAL MACROPHAGE INFLAMMATORY PROTEIN-II) (chains A, B)
GDTLGASWHRPDKCCLGYQKRPLPQVLLSSWYPTSQLCSKPGVIFLTKRGRQVCADKSKD
WVKKLMQQLPVTAR

Primary citation

Comparison of the structure of vMIP-II with eotaxin-1, RANTES, and MCP-3 suggests a unique mechanism for CCR3 activation. Fernandez, E.J., Wilken, J., Thompson, D.A. et al. Biochemistry (2000) 39:12837-12844. DOI 10.1021/bi001166f · PubMed

Other PDB entries of the same protein (UniProt Q98157 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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