2MLO: MCP-1 receptor

Human CCR2 Membrane-Proximal C-Terminal Region (PRO-C) in a Membrane bound form. Determined by solution NMR. Released 8 Oct 2014.

Method: Solution NMR
Organism: Homo sapiens
Chains: 1
Atoms: 151
Mol. weight: 2.13 kDa
Released: 8 Oct 2014

Explore 2MLO in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2MLO contains 1 α-helix and 0 β-strands across 1 chain. 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: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	4-12	9

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
MCP-1 receptor	A	protein	16	Homo sapiens	P41597 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2MLO_1 MCP-1 receptor (chains A)
EKFRRYLSVFFRKHIT

Primary citation

Structural basis for the binding of the membrane-proximal C-terminal region of chemokine receptor CCR2 with the cytosolic regulator FROUNT. Esaki, K., Yoshinaga, S., Tsuji, T. et al. FEBS J (2014) 281:5552-5566. DOI 10.1111/febs.13096 · PubMed

Other PDB entries of the same protein (UniProt P41597 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7P8X 1.4 Å, Crystal Structure of leukotoxin LukE from Staphylococcus aureus in complex with a doubly…
6GPX 2.7 Å, Crystal structure of CCR2A in complex with mk-0812
5T1A 2.81 Å, Structure of CC Chemokine Receptor 2 with Orthosteric and Allosteric Antagonists
7XA3 2.9 Å, Cryo-EM structure of the CCL2 bound CCR2-Gi complex
6GPS 3.3 Å, Crystal structure of CCR2A in complex with mk-0812
2MLQ Human CCR2 Membrane-Proximal C-Terminal Region (PRO-C) in a frount bound form

Browse structure collections

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