3EKJ: Calcium-free GCaMP2

Calcium-free GCaMP2 (calcium binding deficient mutant). Determined by X-ray diffraction at 2.8 Å resolution. Released 16 Dec 2008.

Method: X-ray diffraction
Resolution: 2.8 Å
Organisms: artificial gene, Aequorea victoria, Rattus norvegicus
Chains: 1
Atoms: 2,405
Mol. weight: 50.48 kDa
Released: 16 Dec 2008

Explore 3EKJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3EKJ contains 10 α-helices and 16 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: 10 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	61-68	8	1
β-strand	73-83	11	1
β-strand	84	1	2
β-strand	89-100	12	1
α-helix	108-110	3
β-strand	112-121	10	1
β-strand	130-140	11	1
α-helix	161-164	4
β-strand	170-180	11	1
β-strand	183-194	12	1
β-strand	199-206	8	1
α-helix	215-218	4
α-helix	227-229	3
β-strand	231	1	1
α-helix	234-239	6
α-helix	241-244	4
β-strand	250-258	9	1
β-strand	263-273	11	1
β-strand	276-286	11	1
β-strand	299	1	2
α-helix	309-321	13
β-strand	329-331	3	3
α-helix	335-340	6
α-helix	348-358	11
β-strand	365-367	3	3
α-helix	368-377	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Myosin light chain kinase, Green fluorescent protein, Calmodulin chimera	A	protein	449	artificial gene, Aequorea victoria, Rattus norvegicus	P0DP31 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3EKJ_1 Myosin light chain kinase, Green fluorescent protein, Calmodulin chimera (chains A)
MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDLATMVDSSRRKWNKTGHAVRAIGRLSSL
ENVYIMADKQKNGIKANFKIRHNIEDGGVQLAYHYQQNTPIGDGPVLLPDNHYLSTQSKL
SKDPNEKRDHMVLLEFVTAAGITLGMDELYKGGTGGSMVSKGEELFTGVVPILVELDGDV
NGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLXVQCFSRYPDHMKQHDFF
KSAMPEGYIQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYN
TRDQLTEEQIAEFKEAFSLFDKDGDGGITTKQLGTVMRSLGQNPTEAELQDMINEVGADG
NGTIDFPQFLTMMARKMKDTDSEEEIREAFRVFGKDGNGYISAAQLRHVMTNLGEKLTDE
EVDEMIREAGIDGDGQVNYEQFVQMMTAK

Primary citation

Crystal Structures of the GCaMP Calcium Sensor Reveal the Mechanism of Fluorescence Signal Change and Aid Rational Design. Akerboom, J., Rivera, J.D., Guilbe, M.M. et al. J Biol Chem (2009) 284:6455-6464. DOI 10.1074/jbc.M807657200 · PubMed

Other PDB entries of the same protein (UniProt P0DP31 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3SG6 1.7 Å, Crystal Structure of Dimeric GCaMP2-LIA(linker 1)
3EVU 1.75 Å, Crystal structure of Calcium bound dimeric GCAMP2
3EK7 1.85 Å, Calcium-saturated GCaMP2 dimer
3SG5 1.9 Å, Crystal Structure of Dimeric GCaMP3-D380Y, QP(linker 1), LP(linker 2)
3SG7 1.9 Å, Crystal Structure of GCaMP3-KF(linker 1)
3EKH 2.0 Å, Calcium-saturated GCaMP2 T116V/K378W mutant monomer
3SG2 2.0 Å, Crystal Structure of GCaMP2-T116V,D381Y
3SG3 2.1 Å, Crystal Structure of GCaMP3-D380Y
4I2Y 2.2 Å, Crystal Structure of the genetically encoded calcium indicator RGECO1
3SG4 2.4 Å, Crystal Structure of GCaMP3-D380Y, LP(linker 2)
3WLC 2.49 Å, Crystal structure of dimeric GCaMP6m
3EK4 2.65 Å, Calcium-saturated GCaMP2 Monomer

Browse structure collections

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