1I9I: PDB entry 1I9I

Native crystal structure of the recombinant monoclonal wild type anti-testosterone FAB fragment. Determined by X-ray diffraction at 2.72 Å resolution. Released 20 Mar 2002.

Method: X-ray diffraction
Resolution: 2.72 Å
Organism: Mus musculus
Chains: 2
Atoms: 3,433
Mol. weight: 47.57 kDa
Released: 20 Mar 2002

Explore 1I9I in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1I9I contains 13 α-helices and 43 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: 8 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	6
β-strand	10-12	3	7
β-strand	18-25	8	6
β-strand	34-39	6	7
β-strand	45-51	7	7
β-strand	57-59	3	7
β-strand	67-72	6	6
β-strand	77-82	6	6
α-helix	87-89	3
β-strand	91-98	8	7
β-strand	105-108	4	7
β-strand	112-116	5	7
α-helix	119-121	3
β-strand	122	1	8
α-helix	123-124	2
β-strand	125-129	5	9
β-strand	140-150	11	9
β-strand	151	1	8
β-strand	156	1	10
β-strand	159	1	10
α-helix	160-162	3
β-strand	168-170	3	9
α-helix	171-173	3
β-strand	174-175	2	9
β-strand	180-189	10	9
α-helix	190-192	3
β-strand	199-204	6	10
α-helix	205-207	3
β-strand	209-214	6	10
α-helix	217-219	3

Chain L: 5 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	5-7	3	1
β-strand	10-14	5	2
β-strand	19-24	6	1
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
β-strand	102-103	2	2
β-strand	107-112	6	2
β-strand	116	1	3
β-strand	119-123	5	4
α-helix	127-131	5
β-strand	134-144	11	4
β-strand	145	1	3
β-strand	149-155	7	5
β-strand	158-160	3	5
β-strand	164-168	5	4
α-helix	170-172	3
β-strand	178-187	10	4
α-helix	188-191	4
β-strand	196-203	8	5
β-strand	210-215	6	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Recombinant monoclonal anti-testosterone FAB fragment light chain	L	protein	219	Mus musculus	Q65ZC0 (AlphaFold model)
Recombinant monoclonal anti-testosterone FAB fragment heavy chain	H	protein	220	Mus musculus	Q91Z05 (AlphaFold model)

Sequence of entity 1 (L), FASTA

>1I9I_1 RECOMBINANT MONOCLONAL ANTI-TESTOSTERONE FAB FRAGMENT LIGHT CHAIN (chains L)
DVVVTQTPLSLPVSLGDQASISCRSSQSIVHSNGNSYLEWYLQKPGQSPKLLIYKVSNRF
SGVPDRFSGSGSGTDFTLKISRVEAEDLGVYYCFQGSHVPPTFGGGTKLEIKRADAAPTV
SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSM
SSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC

Sequence of entity 2 (H), FASTA

>1I9I_2 RECOMBINANT MONOCLONAL ANTI-TESTOSTERONE FAB FRAGMENT HEAVY CHAIN (chains H)
EVKLVESGGGLVKPGGSLKLSCAASGFTFSTYALSWVRQTADKRLEWVASIVSGGNTYYS
GSVKGRFTISRDIARNILYLQMSSLRSEDTAMYYCAREYYGYVGLAYWGQGTLVTVSAAK
TTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLY
TLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKIVPRDC

Primary citation

Structural insights into steroid hormone binding: the crystal structure of a recombinant anti-testosterone Fab fragment in free and testosterone-bound forms. Valjakka, J., Takkinenz, K., Teerinen, T. et al. J Biol Chem (2002) 277:4183-4190. DOI 10.1074/jbc.M105579200 · 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.
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)

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