1LO0: If kappa light chain

Catalytic Retro-Diels-Alderase Transition State Analogue Complex. 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: 6,905
Mol. weight: 96.62 kDa
Ligands: BC1
Released: 26 Jun 2002

Explore 1LO0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1LO0 contains 28 α-helices and 88 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, 22 β-strands

Element	Residues	Length	Sheet
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
α-helix	209	1
β-strand	210-215	6	16
β-strand	218	1	16

Chain X: 9 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	2-3	2
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	127-131	5
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: 5 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	67	1	6
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
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	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	P01837 (AlphaFold model)
Ig gamma 2a heavy chain	H, Y	protein	220	Mus musculus	P01865 (AlphaFold model)

Sequence of entity 1 (L, X), FASTA

>1LO0_1 If kappa light chain (chains L, X)
DVLMTQTPLSLPVSLGDQVSIFCTSSQTIVHTNGNTYLEWYLQKPGQSPKLLIYKVSNRF
SGVPDRFSGSGSGTDFTLKISRVETEDLGIYYCFQGSHFPLAFGAGTKLELKRADAAPTV
SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSM
SSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC

Sequence of entity 2 (H, Y), FASTA

>1LO0_2 Ig gamma 2a heavy chain (chains H, Y)
EVKLVESGGGLVKPGGSLKLSCAASGFSFRNYGMSWVRQTPEKRLEWVASISYGGLIYYP
DSIKGRFTISRDIAQNILYLQMSSLRSEDTAMYHCIRGDSFLVWFTFWGQGTLVTVSAAK
TTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLY
TLSSSVTVTSSTWPSQSITCNVAHPASSTQVDKKIEPRGP

Ligands and cofactors

ID	Name	Formula	Copies
BC1	3-{[(9-cyano-9,10-dihydro-10-methylacridin-9-yl)carbonyl]amino}propanoic acid	C19 H17 N3 O3	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 P01837 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3D9A 1.2 Å, High Resolution Crystal Structure Structure of HyHel10 Fab Complexed to Hen Egg Lysozyme
1RUR 1.5 Å, Crystal Structure (I) of native Diels-Alder antibody 13G5 Fab at pH 8.0 with a data set…
2AJU 1.5 Å, Cyrstal structure of cocaine catalytic antibody 7A1 Fab'
2AJV 1.5 Å, Crystal Structure of Cocaine catalytic Antibody 7A1 Fab' in Complex with Cocaine
2W60 1.5 Å, Anti citrullinated Collagen type 2 antibody acc4
2W9D 1.57 Å, Structure of Fab fragment of the ICSM 18 - anti-Prp therapeutic antibody at 1.57 A…
3BKJ 1.59 Å, Crystal structure of Fab wo2 bound to the n terminal domain of amyloid beta peptide (1-16)
3BAE 1.59 Å, Crystal structure of Fab WO2 bound to the N terminal domain of Amyloid beta peptide (1-28)
2R1Y 1.6 Å, Crystal structure of S25-2 Fab in complex with Kdo analogues
2R2B 1.6 Å, Crystal structure of S25-2 Fab in complex with Kdo analogues
3BKM 1.6 Å, Structure of anti-amyloid-beta Fab WO2 (Form A, P212121)
3CFB 1.6 Å, High-resolution structure of blue fluorescent antibody EP2-19G2 in complex with stilbene…

Browse structure collections

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