4LLQ: Mutated CH1

Structure of redesigned IgG1 first constant and lambda domains (CH1:Clambda constant redesign 2 beta, CRD2b) at 1.42A. Determined by X-ray diffraction at 1.42 Å resolution. Released 29 Jan 2014.

Method: X-ray diffraction
Resolution: 1.42 Å
Organism: Homo sapiens
Chains: 2
Atoms: 1,681
Mol. weight: 27.96 kDa
Ligands: PG6
Released: 29 Jan 2014

Explore 4LLQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4LLQ contains 10 α-helices and 25 β-strands across 2 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: 5 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	136	1	1
α-helix	137-138	2
β-strand	139-143	5	2
β-strand	150-151	2	2
β-strand	154-164	11	2
β-strand	165	1	1
β-strand	170-173	4	3
α-helix	174-176	3
β-strand	178	1	3
β-strand	182-184	3	2
α-helix	186-187	2
β-strand	188-189	2	2
β-strand	195-204	10	2
α-helix	205-207	3
β-strand	208	1	4
β-strand	211	1	4
β-strand	214-219	6	3
α-helix	220-222	3
β-strand	224-229	6	3

Chain B: 5 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	115	1	5
α-helix	116-117	2
β-strand	118-122	5	6
α-helix	123-125	3
α-helix	126-130	5
β-strand	134-143	10	6
β-strand	144	1	5
β-strand	149-154	6	7
β-strand	157-159	3	7
β-strand	163-165	3	6
α-helix	166-168	3
β-strand	169-170	2	6
β-strand	176-184	9	6
α-helix	186-191	6
β-strand	195-201	7	7
β-strand	204-210	7	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
mutated CH1	A	protein	113	Homo sapiens	P01857 (AlphaFold model)
mutated light chain Clambda	B	protein	151	Homo sapiens	P0DOY2 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4LLQ_1 mutated CH1 (chains A)
MAASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTGPAVLQ
SSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCGSHHHHHH

Sequence of entity 2 (B), FASTA

>4LLQ_2 mutated light chain Clambda (chains B)
MKYLLPTAAAGLLLLAAQPAMAGQPKAAPSVTLFPPSSEELQANKATLVCAISDFYPGAV
TVAWKADSSPVKAGVETTTPSKQSNNKYAAWSYLSLTPEQWKSHRSYSCQVTHEGSTVEK
TVAPTECLESGKETAAAKFERQHMDSSTSAA

Ligands and cofactors

ID	Name	Formula	Copies
PG6	1-(2-methoxy-ethoxy)-2-{2-[2-(2-methoxy-ethoxy]-ethoxy}-ethane	C12 H26 O6	1

Primary citation

Generation of bispecific IgG antibodies by structure-based design of an orthogonal Fab interface. Lewis, S.M., Wu, X., Pustilnik, A. et al. Nat Biotechnol (2014) 32:191-198. DOI 10.1038/nbt.2797 · PubMed

Other PDB entries of the same protein (UniProt P01857 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4LLD 1.19 Å, Structure of wild-type IgG1 antibody heavy chain constant domain 1 and light chain…
3TV3 1.29 Å, Crystal structure of broad and potent HIV-1 neutralizing antibody PGT128 in complex with…
5HSF 1.52 Å, 1.52 Angstrom Crystal Structure of Fc fragment of Human IgG1.
6YT7 1.55 Å, Glycosylated knob/dummy-hole fc fragment
4NWU 1.6 Å, Crystal structure of APE1551, an anti-human NGF Fab with a nine amino acid insertion in…
1L6X 1.65 Å, Fc fragment of rituximab bound to a minimized version of the B-domain from protein A…
3TWC 1.65 Å, Crystal structure of broad and potent HIV-1 neutralizing antibody PGT127 in complex with…
5JIH 1.66 Å, Crystal structure of HER2 binding IgG1-Fc (Fcab STAB19)
3MCL 1.7 Å, Anti-beta-amyloid antibody c706 fab in space group P21
5U66 1.7 Å, Modified single helix from the B-domain of protein A bound to IgG1 Fc
6N35 1.75 Å, Anti-HIV-1 Fab 2G12 + Man1-2 re-refinement
3DJ9 1.75 Å, Crystal Structure of an isolated, unglycosylated antibody CH2 domain

Browse structure collections

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