1DOM: MCP-1

Solution structure of the monocyte chemoattractant protein-1 dimer using heteronuclear, NMR, minimized average structure. Determined by solution NMR. Released 14 Oct 1996.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
1,214
Mol. weight
17.4 kDa
Released
14 Oct 1996

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

Secondary structure: helices and β-sheets

1DOM contains 2 α-helices and 12 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, 6 β-strands

ElementResiduesLengthSheet
β-strand9-1131
β-strand27-2822
β-strand3113
β-strand4013
β-strand41-4442
β-strand50-5342
α-helix60-689

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
MCP-1A, Bprotein76Homo sapiensP13500 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1DOM_1 MCP-1 (chains A, B)
QPDAINAPVTCCYNFTNRKISVQRLASYRRITSSKCPKEAVIFKTIVAKEICADPKQKWV
QDSMDHLDKQTQTPKT

Primary citation

Heteronuclear (1H, 13C, 15N) NMR assignments and solution structure of the monocyte chemoattractant protein-1 (MCP-1) dimer. Handel, T.M., Domaille, P.J. Biochemistry (1996) 35:6569-6584. DOI 10.1021/bi9602270 · PubMed

Other PDB entries of the same protein (UniProt P13500 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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