6C6M: IgCam3 of human MLCK1

IgCam3 of human MLCK1. Determined by X-ray diffraction at 2.5 Å resolution. Released 23 Jan 2019.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Homo sapiens
Chains: 3
Atoms: 2,302
Mol. weight: 34.9 kDa
Released: 23 Jan 2019

Explore 6C6M in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6C6M contains 8 α-helices and 32 β-strands across 3 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.

Chain A: 2 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	415-418	4	1
α-helix	419-422	4
β-strand	423-425	3	2
β-strand	431-435	5	3
β-strand	436-438	3	1
β-strand	444-449	6	2
β-strand	452-453	2	2
β-strand	461-466	6	3
β-strand	469-474	6	3
α-helix	479-481	3
β-strand	483-491	9	2
β-strand	494-504	11	2

Chain B: 3 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	415-418	4	4
α-helix	419-422	4
β-strand	423-426	4	5
β-strand	431-435	5	6
β-strand	436-438	3	4
α-helix	443	1
β-strand	444-449	6	5
β-strand	452-454	3	5
β-strand	457	1	6
β-strand	461-466	6	6
β-strand	469-474	6	6
α-helix	479-481	3
β-strand	483-490	8	5
β-strand	495-505	11	5

Chain C: 3 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	415-418	4	7
α-helix	419-422	4
β-strand	423-426	4	8
β-strand	431-435	5	9
β-strand	436-438	3	7
α-helix	442-443	2
β-strand	444-449	6	8
β-strand	452-453	2	8
β-strand	457	1	9
β-strand	461-465	5	9
β-strand	470-474	5	9
α-helix	479-481	3
β-strand	483-490	8	8
β-strand	495-505	11	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Myosin light chain kinase, smooth muscle	A, B, C	protein	103	Homo sapiens	Q15746 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>6C6M_1 Myosin light chain kinase, smooth muscle (chains A, B, C)
MEGQRDSAFPKFESKPQSQEVKENQTVKFRCEVSGIPKPEVAWFLEGTPVRRQEGSIEVY
EDAGSHYLCLLKARTRDSGTYSCTASNAQGQLSCSWTLQVERL

Primary citation

Intracellular MLCK1 diversion reverses barrier loss to restore mucosal homeostasis. Graham, W.V., He, W., Marchiando, A.M. et al. Nat Med (2019) 25:690-700. DOI 10.1038/s41591-019-0393-7 · PubMed

Other PDB entries of the same protein (UniProt Q15746 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9MXD 1.17 Å, Human E104A calmodulin:MLCK RM20 complex
9MVW 1.58 Å, Crystal structure of S101F calmodulin - CaM:RM20 analog complex
5JQA 1.8 Å, CaM:RM20 complex
5JTH 1.84 Å, Crystal structure of E67A calmodulin - CaM:RM20 analog complex
2CQV Solution structure of the eighth Ig-like domain of human myosin light chain kinase
2YR3 Solution structure of the fourth Ig-like domain from myosin light chain kinase, smooth…

Browse structure collections

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