6K64: 3LRH intrabody

Application of anti-helix antibodies in protein structure determination (8188-3LRH). Determined by X-ray diffraction at 1.93 Å resolution. Released 14 Aug 2019.

Method: X-ray diffraction
Resolution: 1.93 Å
Organisms: Homo sapiens, Staphylococcus aureus subsp. aureus
Chains: 4
Atoms: 2,716
Mol. weight: 46.12 kDa
Released: 14 Aug 2019

Explore 6K64 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6K64 contains 15 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 B: 3 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	7	1	1
β-strand	8-9	2	2
α-helix	10-12	3
β-strand	13-15	3	3
β-strand	21-26	6	2
β-strand	37-42	6	3
β-strand	49-53	5	3
β-strand	57-58	2	3
α-helix	59	1
β-strand	66-71	6	2
β-strand	74-79	6	2
α-helix	84-86	3
β-strand	88-96	9	3
β-strand	101-104	4	3
β-strand	105	1	1
β-strand	108-112	5	3

Chain C: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	2805-2815	11
α-helix	2822-2834	13
α-helix	2836-2838	3
α-helix	2839-2853	15
α-helix	2855-2858	4

Chain H: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	5-15	11
α-helix	22-34	13
α-helix	36-38	3
α-helix	39-58	20

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
3LRH intrabody	A, B	protein	135	Homo sapiens
Protein A	C, H	protein	79	Staphylococcus aureus subsp. aureus	P02976 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6K64_1 3LRH intrabody (chains A, B)
MGSSHHHHHHSSGLVPRGSHMGSQPVLTQSPSVSAAPRQRVTISVSGSNSNIGSNTVNWI
QQLPGRAPELLMYDDDLLAPGVSDRFSGSRSGTSASLTISGLQSEDEADYYAATWDDSLN
GWVFGGGTKVTVLSA

Sequence of entity 2 (C, H), FASTA

>6K64_2 Protein A (chains C, H)
MGSSHHHHHHSSGLVPRGSHMFNKDQQSAFYEILNMPNLNEAQRNGFIQSLKDDPSQSTN
VLGEAKKLNKAQASLKSFQ

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 P02976 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8DA5 1.0 Å, Coevolved affibody-Z domain pair LL1.c4
8DA7 1.02 Å, Coevolved affibody-Z domain pair LL1.c6
8DA3 1.06 Å, Coevolved affibody-Z domain pair LL1.c1
8DAB 1.13 Å, Coevolved affibody-Z domain pair LL2.c17
8DAC 1.19 Å, Coevolved affibody-Z domain pair LL2.c22
8DA8 1.29 Å, Coevolved affibody-Z domain pair LL2.c1
8DA9 1.35 Å, Coevolved affibody-Z domain pair LL2.c3
9M6O 1.49 Å, Crystal structure of S. aureus protein A bound to a camelid single-domain antibody
8DA6 1.5 Å, Coevolved affibody-Z domain pair LL1.c5
6K65 1.65 Å, Application of anti-helix antibodies in protein structure determination (9014-1P4B)
5U6A 1.74 Å, Crystal structure of I83E meditope-enabled trastuzumab with azido-PEG3-meditope
8DAA 1.75 Å, Coevolved affibody-Z domain pair LL2.c7

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