1B50: Human mip-1A D26A, 10 structures

NMR structure of human mip-1A D26A, 10 structures. Determined by solution NMR. Released 22 Jul 1999.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
1,076
Mol. weight
15.36 kDa
Released
22 Jul 1999

Explore 1B50 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1B50 contains 2 α-helices and 4 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: 1 helix, 2 β-strands

ElementResiduesLengthSheet
β-strand26-2831
β-strand40-4231
α-helix56-616

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Mip-1AA, Bprotein69Homo sapiensP10147 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1B50_1 MIP-1A (chains A, B)
SLAADTPTACCFSYTSRQIPQNFIAAYFETSSQCSKPGVIFLTKRSRQVCADPSEEWVQK
YVSDLELSA

Primary citation

Identification of amino acid residues critical for aggregation of human CC chemokines macrophage inflammatory protein (MIP)-1alpha, MIP-1beta, and RANTES. Characterization of active disaggregated chemokine variants. Czaplewski, L.G., McKeating, J., Craven, C.J. et al. J Biol Chem (1999) 274:16077-16084. DOI 10.1074/jbc.274.23.16077 · PubMed

Other PDB entries of the same protein (UniProt P10147 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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