6K67: 3LRH introbody

Application of anti-helix antibodies in protein structure determination (9011-3LRH). Determined by X-ray diffraction at 1.95 Å resolution. Released 14 Aug 2019.

Method: X-ray diffraction
Resolution: 1.95 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,146
Mol. weight: 51.94 kDa
Ligands: CA
Released: 14 Aug 2019

Explore 6K67 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6K67 contains 14 α-helices and 26 β-strands across 4 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 and C: 3 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	5-6	2	1
α-helix	7-9	3
β-strand	10-12	3	2
β-strand	18-23	6	1
β-strand	35-39	5	2
β-strand	46-50	5	2
β-strand	54-55	2	2
α-helix	56	1
β-strand	63-68	6	1
β-strand	71-76	6	1
α-helix	81-83	3
β-strand	85-93	9	2
β-strand	98-101	4	2
β-strand	105-109	5	2

Chain B: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	3-26	24
β-strand	34	1	3
α-helix	36-45	10
α-helix	52-60	9
β-strand	70	1	3
α-helix	72-82	11

Chain D: 4 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	3-26	24
β-strand	34	1	6
α-helix	36-45	10
α-helix	52-60	9
β-strand	70	1	6
α-helix	72-81	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
3LRH introbody	A, C	protein	135	Homo sapiens
Engineered calmodulin	B, D	protein	104	Homo sapiens	P0DP25 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>6K67_1 3LRH introbody (chains A, C)
MGSSHHHHHHSSGLVPRGSHMGSQPVLTQSPSVSAAPRQRVTISVSGSNSNIGSNTVNWI
QQLPGRAPELLMYDDDLLAPGVSDRFSGSRSGTSASLTISGLQSEDEADYYAATWDDSLN
GWVFGGGTKVTVLSA

Sequence of entity 2 (B, D), FASTA

>6K67_2 Engineered calmodulin (chains B, D)
MGSSHHHHHHSSGLVPRGSHMEKLMKAFESLQIFQFKEAFSLFDKDGDGTITTKELGTVM
RSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTD

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	4

Primary citation

Application of antihelix antibodies in protein structure determination. Kim, J.W., Kim, S., Lee, H. et al. Proc Natl Acad Sci U S A (2019) 116:17786-17791. DOI 10.1073/pnas.1910080116 · PubMed

Other PDB entries of the same protein (UniProt P0DP25 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7BYL 2.5 Å, Cryo-EM structure of human KCNQ4
7XNN 2.5 Å, human KCNQ1-CaM-ML277-PIP2 complex in state B
7XNK 2.6 Å, human KCNQ1-CaM in complex with ML277
7VNP 2.79 Å, Structure of human KCNQ4-ML213 complex with PIP2
7VNR 2.8 Å, Structure of human KCNQ4-ML213 complex in digitonin
9LJ5 2.9 Å, Human KCNQ5-CaM-PIP2-HN37 complex in an open conformation.
7VNQ 2.96 Å, Structure of human KCNQ4-ML213 complex in nanodisc
7BYM 3.1 Å, Cryo-EM structure of human KCNQ4 with retigabine
7XNL 3.1 Å, human KCNQ1-CaM-ML277-PIP2 complex in state A
9IXY 3.1 Å, Human KCNQ2-CaM-Ebio2 Complex in the Presence of PIP2
9LIZ 3.1 Å, Human KCNQ5-CaM in complex with PIP2
9LJ1 3.2 Å, Human KCNQ5-CaM-PIP2-HN37 complex in a closed conformation.

Browse structure collections

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