1LO2: Retro-Diels-Alderase Catalytic Antibody

Retro-Diels-Alderase Catalytic Antibody. Determined by X-ray diffraction at 2.0 Å resolution. Released 26 Jun 2002.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Mus musculus
Chains: 4
Atoms: 6,934
Mol. weight: 96.54 kDa
Ligands: OX1
Released: 26 Jun 2002

Explore 1LO2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1LO2 contains 28 α-helices and 87 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.

Chain H: 6 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	17
β-strand	11-12	2	18
β-strand	18-25	8	17
β-strand	33-39	7	19
β-strand	45-51	7	19
β-strand	60-61	2	19
β-strand	71-75	5	17
β-strand	80-85	6	17
α-helix	90-92	3
β-strand	94-102	9	19
β-strand	104B-109	6	19
β-strand	113-115	3	19
β-strand	116-117	2	18
β-strand	123	1	20
β-strand	126-130	5	21
α-helix	131-133	3
β-strand	141-151	11	21
β-strand	152	1	20
β-strand	157-160	4	22
α-helix	161-163	3
β-strand	169-171	3	21
α-helix	172-174	3
β-strand	175-176	2	21
β-strand	181-190	10	21
α-helix	191-193	3
β-strand	200-205	6	22
α-helix	206-208	3
β-strand	210-215	6	22

Chain L: 8 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	2-3	2
β-strand	4-7	4	12
β-strand	10-13	4	13
β-strand	19-25	7	12
β-strand	38-43	6	13
β-strand	49-54	6	13
β-strand	58-59	2	13
α-helix	60	1
β-strand	67-72	6	12
β-strand	75-80	6	12
α-helix	85-87	3
β-strand	89-95	7	13
α-helix	101	1
β-strand	102-103	2	13
β-strand	107-111	5	13
β-strand	116	1	14
β-strand	119-123	5	15
α-helix	124-126	3
α-helix	127-131	5
β-strand	134-144	11	15
β-strand	145	1	14
β-strand	150-155	6	16
β-strand	158-159	2	16
β-strand	164-168	5	15
α-helix	169-172	4
β-strand	178-187	10	15
α-helix	188-192	5
β-strand	196-202	7	16
β-strand	210-215	6	16

Chain X: 8 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	1
β-strand	10-13	4	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	107-111	5	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	158-159	2	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

Chain Y: 6 helices, 23 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	60-61	2	8
β-strand	70-75	6	6
β-strand	80-85	6	6
α-helix	90-92	3
β-strand	94-102	9	8
β-strand	104B-109	6	8
β-strand	113-115	3	8
β-strand	116-117	2	7
β-strand	123	1	9
α-helix	124-125	2
β-strand	126-130	5	10
α-helix	131-133	3
β-strand	141-151	11	10
β-strand	152	1	9
β-strand	157-160	4	11
α-helix	161-163	3
β-strand	165	1	11
β-strand	169-171	3	10
α-helix	172-174	3
β-strand	175-176	2	10
β-strand	181-190	10	10
β-strand	200-205	6	11
α-helix	206-208	3
β-strand	210-215	6	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
If kappa light chain	L, X	protein	219	Mus musculus	Q65ZC0 (AlphaFold model)
Ig gamma 2a heavy chain	H, Y	protein	220	Mus musculus	Q91Z05 (AlphaFold model)

Sequence of entity 1 (L, X), FASTA

>1LO2_1 If kappa light chain (chains L, X)
DVLMTQTPLSLPVSLGDQVSIFCTSSQTIVHTNGNTYLEWYLQKPGQSPKLLIYKVSNRF
SGVPDRFSGSGSGTDFTLKISRVETEDLGIYYCFQGSHFPLAFGAGTKLELKRADAAPTV
SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSM
SSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC

Sequence of entity 2 (H, Y), FASTA

>1LO2_2 Ig gamma 2a heavy chain (chains H, Y)
EVKLVESGGGLVKPGGSLKLSCAASGFSFRNYGMSWVRQTPEKRLEWVASISYGGLIYYP
DSIKGRFTISRDIAQNILYLQMSSLRSEDTAMYHCIRGDSFLVWFTFWGQGTLVTVSAAK
TTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLY
TLSSSVTVTSSTWPSQSITCNVAHPASSTQVDKKIEPRGP

Ligands and cofactors

ID	Name	Formula	Copies
OX1	[2'-carboxylethyl]-10-methyl-anthracene endoperoxide	C18 H16 O4	2

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
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.
1LO4 2.4 Å, Retro-Diels-Alderase Catalytic antibody 9D9
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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