6UZZ: Human KCNQ1-CaM complex

structure of human KCNQ1-CaM complex. Determined by electron microscopy at 3.1 Å resolution. Released 4 Dec 2019.

Method: Electron microscopy
Resolution: 3.1 Å
Organism: Homo sapiens
Chains: 8
Atoms: 15,832
Mol. weight: 320.77 kDa
Ligands: CA
Released: 4 Dec 2019

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

Secondary structure: helices and β-sheets

6UZZ contains 128 α-helices and 8 β-strands across 8 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.

Chains A, C, E and G: 22 helices, 0 β-strands

Element	Residues	Length
α-helix	105-114	10
α-helix	121-142	22
α-helix	151-154	4
α-helix	157-177	21
α-helix	178-180	3
α-helix	187-193	7
α-helix	197-215	19
α-helix	224-236	13
α-helix	237-240	4
α-helix	246-257	12
α-helix	259-284	26
α-helix	299-310	12
α-helix	323-335	13
α-helix	338-357	20
α-helix	358-360	3
α-helix	361-363	3
α-helix	364-367	4
α-helix	368-383	16
α-helix	390-394	5
α-helix	510-531	22
α-helix	535-536	2
α-helix	538-566	29

Chains B, D, F and H: 10 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	7-21	15
α-helix	30-39	10
α-helix	46-53	8
α-helix	66-74	9
α-helix	80-90	11
α-helix	91-93	3
β-strand	100-102	3	1
α-helix	103-112	10
α-helix	116-118	3
α-helix	119-127	9
β-strand	136-138	3	1
α-helix	139-146	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Potassium voltage-gated channel subfamily KQT member 1	A, C, E, G	protein	557	Homo sapiens	P51787 (AlphaFold model)
Calmodulin-1	B, D, F, H	protein	149	Homo sapiens	P0DP23 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>6UZZ_1 Potassium voltage-gated channel subfamily KQT member 1 (chains A, C, E, G)
MASDLGPRPPVSLDPRVSIYSTRRPVLARTHVQGRVYNFLERPTGWKCFVYHFAVFLIVL
VCLIFSVLSTIEQYAALATGTLFWMEIVLVVFFGTEYVVRLWSAGCRSKYVGLWGRLRFA
RKPISIIDLIVVVASMVVLCVGSKGQVFATSAIRGIRFLQILRMLHVDRQGGTWRLLGSV
VFIHRQELITTLYIGFLGLIFSSYFVYLAEKDAVNESGRVEFGSYADALWWGVVTVTTIG
YGDKVPQTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQKHFNRQIPAAASL
IQTAWRCYAAENPDSSTWKIYIRKAPRSHTLLSPSPKPKKSVVVKKKKFKLDKDNGVTPG
EKMLTVPHITCDPPEERRLDHFSVDGYDSSVRKSPTLLEVSMPHFMRTNSFAEDLDLEGE
TLLTPITHISQLREHHRATIKVIRRMQYFVAKKKFQQARKPYDVRDVIEQYSQGHLNLMV
RIKELQRRLDQSIGKPSLFISVSEKSKDRGSNTIGARLNRVEDKVTQLDQRLALITDMLH
QLLSLHSNSLEVLFQGP

Sequence of entity 2 (B, D, F, H), FASTA

>6UZZ_2 Calmodulin-1 (chains B, D, F, H)
MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG
NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE
EVDEMIREADIDGDGQVNYEEFVQMMTAK

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	8

Primary citation

Structural Basis of Human KCNQ1 Modulation and Gating. Sun, J., MacKinnon, R. Cell (2020) 180:340-347.e9. DOI 10.1016/j.cell.2019.12.003 · PubMed

Other PDB entries of the same protein (UniProt P51787 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3HFE 1.7 Å, A trimeric form of the Kv7.1 A domain Tail
3BJ4 2.0 Å, The KCNQ1 (Kv7.1) C-terminus, a multi-tiered scaffold for subunit assembly and protein…
7VVH 2.3 Å, Crystal Structure of the Kv7.1 C-terminal Domain in Complex with Calmodulin disease…
3HFC 2.45 Å, A trimeric form of the Kv7.1 A domain Tail, L602M/L606M mutant Semet
7XNN 2.5 Å, human KCNQ1-CaM-ML277-PIP2 complex in state B
9UJ4 2.59 Å, Structure of human KCNQ1-CaM complex
7XNK 2.6 Å, human KCNQ1-CaM in complex with ML277
7VUO 2.68 Å, Crystal Structure of the Kv7.1 C-terminal Domain in Complex with Calmodulin disease…
9VEC 2.7 Å, structure of human KCNQ1-KCNE1-CaM complex
4V0C 2.86 Å, Crystal Structure of the Kv7.1 proximal C-terminal Domain in Complex with Calmodulin
8SIK 2.9 Å, KCNQ1 with voltage sensor in the up conformation
9U7F 2.9 Å, structure of human KCNQ1-KCNE1-CaM complex

Browse structure collections

About this viewer

MolViewer shows 6UZZ directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.