2MA2: RasGRP2 EF hands

Solution structure of RasGRP2 EF hands bound to calcium. Determined by solution NMR. Released 21 Aug 2013.

Method: Solution NMR
Organism: Homo sapiens
Chains: 1
Atoms: 647
Mol. weight: 9.22 kDa
Released: 21 Aug 2013

Explore 2MA2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2MA2 contains 4 α-helices 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: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	420-437	18
α-helix	448-454	7
α-helix	464-467	4
α-helix	477-486	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
RAS guanyl-releasing protein 2	A	protein	81	Homo sapiens	Q7LDG7 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2MA2_1 RAS guanyl-releasing protein 2 (chains A)
KLDQALVVEHIEKMVESVFRNFDVDGDGHISQEEFQIIRGNFPYLSAFGDLDQNQDGCIS
REEMVSYFLRSSSVLGGRMGF

Primary citation

Structural analysis of autoinhibition in the Ras-specific exchange factor RasGRP1. Iwig, J.S., Vercoulen, Y., Das, R. et al. Elife (2013) 2:e00813-e00813. DOI 10.7554/eLife.00813 · PubMed

Other PDB entries of the same protein (UniProt Q7LDG7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6AXF 3.1 Å, Structure of RasGRP2 in complex with Rap1B

Browse structure collections

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