1L7T: Anti-testosterone

Crystal Structure Analysis of the anti-testosterone Fab fragment. Determined by X-ray diffraction at 2.1 Å resolution. Released 2 Oct 2002.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Mus musculus
Chains: 2
Atoms: 3,643
Mol. weight: 47.74 kDa
Released: 2 Oct 2002

Explore 1L7T in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1L7T contains 14 α-helices and 47 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, 26 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	6
β-strand	11-12	2	7
β-strand	18-25	8	6
α-helix	29-31	3
β-strand	34-39	6	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	91-97	7	8
β-strand	100	1	10
β-strand	103	1	10
β-strand	106	1	8
β-strand	112-114	3	8
β-strand	115-116	2	7
α-helix	120-121	2
β-strand	122	1	11
β-strand	125-129	5	12
β-strand	140-150	11	12
β-strand	151	1	11
β-strand	156-159	4	13
α-helix	160-162	3
β-strand	168-170	3	12
α-helix	171-173	3
β-strand	174-175	2	12
β-strand	180-189	10	12
β-strand	199-204	6	13
α-helix	205-207	3
β-strand	209-214	6	13

Chain L: 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
α-helix	28-30	3
β-strand	38-43	6	2
β-strand	50-54	5	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
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	158-160	3	5
β-strand	164-168	5	4
α-helix	169-172	4
β-strand	178-187	10	4
α-helix	188-192	5
β-strand	196-202	7	5
β-strand	210-215	6	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
anti-testosterone (light chain)	L	protein	219	Mus musculus	Q65ZC0 (AlphaFold model)
anti-testosterone (heavy chain)	H	protein	221	Mus musculus	Q91Z05 (AlphaFold model)

Sequence of entity 1 (L), FASTA

>1L7T_1 anti-testosterone (light chain) (chains L)
DVVVTQTPLSLPVSLGDQASISCRSSEVIVTRNGYTPIEWYLQKPGQSPKLLIYKAYKRF
PGVPDRFSGSGSGTDFTLKISRVEAEDLGVYYCFDGSTVPPKFGGGTKLEIKRADAAPTV
SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSM
SSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRDEC

Sequence of entity 2 (H), FASTA

>1L7T_2 anti-testosterone (heavy chain) (chains H)
EVKLVESGGGLVKPGGSLKLSCAASGFTFSRYALSWVRQTADKRLEWVASIVSGGNTYYS
GSVKGRFTISRDIARNILYLQMSSLRSEDTAMYYCARAYYGYVGLVHWGQGTLVTVSSAK
TTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLY
TLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKIVPRDCG

Primary citation

Crystal Structure of an in Vitro Affinity- and Specificity-matured Anti-testosterone Fab in Complex with Testosterone. IMPROVED AFFINITY RESULTS FROM SMALL STRUCTURAL CHANGES WITHIN THE VARIABLE DOMAINS. Valjakka, J., Hemminki, A., Niemi, S. et al. J Biol Chem (2002) 277:44021-44027. DOI 10.1074/jbc.M208392200 · 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
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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