1LO4: Retro-Diels-Alderase Catalytic antibody 9D9

Retro-Diels-Alderase Catalytic antibody 9D9. Determined by X-ray diffraction at 2.4 Å resolution. Released 3 Jul 2002.

Method: X-ray diffraction
Resolution: 2.4 Å
Organism: Mus musculus
Chains: 2
Atoms: 3,371
Mol. weight: 47.65 kDa
Released: 3 Jul 2002

Explore 1LO4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1LO4 contains 14 α-helices and 46 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 H: 6 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	6
β-strand	11-12	2	7
β-strand	18-25	8	6
β-strand	33-39	7	8
β-strand	45-51	7	8
β-strand	57-59	3	8
β-strand	64	1	9
β-strand	67	1	9
β-strand	68-72	5	6
β-strand	77-82	6	6
α-helix	87-89	3
β-strand	91-99	9	8
β-strand	103-108	6	8
β-strand	112-114	3	8
β-strand	115-116	2	7
α-helix	119-121	3
β-strand	122	1	10
α-helix	123-124	2
β-strand	125-129	5	11
β-strand	140-150	11	11
β-strand	151	1	10
β-strand	156-159	4	12
α-helix	160-162	3
β-strand	164	1	12
β-strand	168-170	3	11
α-helix	171-173	3
β-strand	174-176	3	11
β-strand	179-189	11	11
β-strand	199-204	6	12
α-helix	205-207	3
β-strand	209-214	6	12

Chain L: 8 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	1
β-strand	10-14	5	2
β-strand	19-25	7	1
β-strand	38-43	6	2
β-strand	49-54	6	2
β-strand	58-59	2	2
α-helix	60	1
β-strand	67-72	6	1
β-strand	75-80	6	1
α-helix	85-87	3
β-strand	89-95	7	2
α-helix	101	1
β-strand	102-103	2	2
β-strand	107-112	6	2
β-strand	116	1	3
α-helix	117-118	2
β-strand	119-123	5	4
α-helix	124-126	3
α-helix	127-132	6
β-strand	134-144	11	4
β-strand	145	1	3
β-strand	150-155	6	5
β-strand	158-160	3	5
β-strand	164-168	5	4
α-helix	169-172	4
β-strand	178-187	10	4
α-helix	188-191	4
β-strand	196-202	7	5
β-strand	210-215	6	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
If kappa light chain	L	protein	217	Mus musculus	Q65ZC0 (AlphaFold model)
Ig gamma 2a heavy chain	H	protein	220	Mus musculus	Q91Z05 (AlphaFold model)

Sequence of entity 1 (L), FASTA

>1LO4_1 If kappa light chain (chains L)
DVLLTQTPLSLPVSLGDQASISCRSSQTIVHTNGNTYFEWYLQKPGQSPHLLIYKVSNRL
SGVPDRFSGSGSGTDFTLKISRVEAEDLGLYYCFQGSHSPWTFGGGTKLELKRADAAPTV
SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSM
SSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRN

Sequence of entity 2 (H), FASTA

>1LO4_2 Ig gamma 2a heavy chain (chains H)
ELKLVETGGDLVKPGGSLTLSCEASGFTLRTYGMSWVRQTPQMRLEWVASISYGGLLYFS
DSVKGRFTISRDIVRNILTLQMSRLRSEDTAIYYCARGTSFVRYFDVWGAGTTVTVSSAK
TTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLY
TLSSSVTVTSSTWPSQSITCNVAHPASSTQVDKKIVPRAA

Primary citation

A structural basis for the activity of retro-Diels-Alder catalytic antibodies: evidence for a catalytic aromatic residue. Hugot, M., Bensel, N., Vogel, M. et al. Proc Natl Acad Sci U S A (2002) 99:9674-9678. DOI 10.1073/pnas.142286599 · PubMed

Other PDB entries of the same protein (UniProt Q65ZC0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2G60 1.85 Å, Structure of anti-FLAG M2 Fab domain
1LO2 2.0 Å, Retro-Diels-Alderase Catalytic Antibody
1L7T 2.1 Å, Crystal Structure Analysis of the anti-testosterone Fab fragment
1LO3 2.3 Å, Retro-Diels-Alderase Catalytic Antibody: Product Analogue
1T66 2.3 Å, The structure of FAB with intermediate affinity for fluorescein.
2GK0 2.45 Å, Structure of Catalytic Elimination Antibody 13G5 from a twinned crystal in space group C2
1I9J 2.6 Å, Testosterone complex structure of the recombinant monoclonal wild type anti-testosterone…
2GJZ 2.65 Å, Structure of Catalytic Elimination Antibody 13G5 from a crystal in space group P2(1)
1I9I 2.72 Å, Native crystal structure of the recombinant monoclonal wild type anti-testosterone FAB…

Browse structure collections

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