3EKH: PDB entry 3EKH

Calcium-saturated GCaMP2 T116V/K378W mutant monomer. Determined by X-ray diffraction at 2.0 Å resolution. Released 16 Dec 2008.

Method: X-ray diffraction
Resolution: 2.0 Å
Organisms: artificial gene, Aequorea victoria, Rattus norvegicus
Chains: 1
Atoms: 3,472
Mol. weight: 51.01 kDa
Ligands: CA
Released: 16 Dec 2008

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

Secondary structure: helices and β-sheets

3EKH contains 17 α-helices and 18 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: 17 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	40-58	19
β-strand	63-68	6	1
α-helix	69-71	3
β-strand	73-83	11	1
β-strand	84	1	2
β-strand	89-100	12	1
α-helix	107-110	4
β-strand	112-121	10	1
β-strand	130-140	11	1
α-helix	162-166	5
β-strand	169-180	12	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	309-322	14
β-strand	329-330	2	3
α-helix	332-341	10
α-helix	348-356	9
β-strand	366-367	2	3
α-helix	368-379	12
α-helix	382-384	3
α-helix	385-395	11
β-strand	402-403	2	4
α-helix	405-414	10
α-helix	421-431	11
β-strand	439-440	2	4
α-helix	441-447	7

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

>3EKH_1 Myosin light chain kinase, Green fluorescent protein, Calmodulin chimera (chains A)
MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDLATMVDSSRRKWNKTGHAVRAIGRLSSL
ENVYIMADKQKNGIKANFKIRHNIEDGGVQLAYHYQQNTPIGDGPVLLPDNHYLSVQSKL
SKDPNEKRDHMVLLEFVTAAGITLGMDELYKGGTGGSMVSKGEELFTGVVPILVELDGDV
NGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTLXVQCFSRYPDHMKQHDFF
KSAMPEGYIQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYN
TRDQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG
NGTIDFPEFLTMMARWMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE
EVDEMIREADIDGDGQVNYEEFVQMMTAK

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	4

Water and common crystallization additives (GOL) are not listed.

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)
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
3WLD 2.7 Å, Crystal structure of monomeric GCaMP6m

Browse structure collections

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