Testosterone complex structure of the recombinant monoclonal wild type anti-testosterone FAB fragment. Determined by X-ray diffraction at 2.6 Å resolution. Released 20 Mar 2002.
Explore 1I9J in 3D Show helices and sheets RCSB PDB PDBe
1I9J 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 7 |
| β-strand | 11-12 | 2 | 8 |
| β-strand | 18-25 | 8 | 7 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 9 |
| β-strand | 45-51 | 7 | 9 |
| β-strand | 57-59 | 3 | 9 |
| β-strand | 64 | 1 | 7 |
| β-strand | 67-72 | 6 | 7 |
| β-strand | 77-82 | 6 | 7 |
| α-helix | 87-89 | 3 | |
| β-strand | 91-100 | 10 | 9 |
| β-strand | 103-108 | 6 | 9 |
| β-strand | 112-114 | 3 | 9 |
| β-strand | 115-116 | 2 | 8 |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 10 |
| 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 | 174-175 | 2 | 11 |
| β-strand | 180-189 | 10 | 11 |
| β-strand | 199-204 | 6 | 12 |
| α-helix | 205-207 | 3 | |
| β-strand | 209-214 | 6 | 12 |
| α-helix | 215 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 1 |
| β-strand | 10-14 | 5 | 2 |
| β-strand | 19-25 | 7 | 1 |
| β-strand | 30 | 1 | 3 |
| β-strand | 36 | 1 | 3 |
| 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 | 4 |
| β-strand | 119-123 | 5 | 5 |
| α-helix | 124-126 | 3 | |
| α-helix | 127-132 | 6 | |
| β-strand | 134-144 | 11 | 5 |
| β-strand | 145 | 1 | 4 |
| β-strand | 150-155 | 6 | 6 |
| β-strand | 158-159 | 2 | 6 |
| β-strand | 164-168 | 5 | 5 |
| α-helix | 169-172 | 4 | |
| β-strand | 178-187 | 10 | 5 |
| α-helix | 188-191 | 4 | |
| β-strand | 196-202 | 7 | 6 |
| β-strand | 210-215 | 6 | 6 |
| 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) |
>1I9J_1 RECOMBINANT MONOCLONAL ANTI-TESTOSTERONE FAB FRAGMENT LIGHT CHAIN (chains L) DVVVTQTPLSLPVSLGDQASISCRSSQSIVHSNGNSYLEWYLQKPGQSPKLLIYKVSNRF SGVPDRFSGSGSGTDFTLKISRVEAEDLGVYYCFQGSHVPPTFGGGTKLEIKRADAAPTV SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSM SSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC
>1I9J_2 RECOMBINANT MONOCLONAL ANTI-TESTOSTERONE FAB FRAGMENT HEAVY CHAIN (chains H) EVKLVESGGGLVKPGGSLKLSCAASGFTFSTYALSWVRQTADKRLEWVASIVSGGNTYYS GSVKGRFTISRDIARNILYLQMSSLRSEDTAMYYCAREYYGYVGLAYWGQGTLVTVSAAK TTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLY TLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKIVPRDC
| ID | Name | Formula | Copies |
|---|---|---|---|
| TES | Testosterone | C19 H28 O2 | 1 |
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:
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