9DL0: Synthetic Fab
Crystal structure of a synthetic Fab (R3H8) in complex with the FRB domain of mTOR. Determined by X-ray diffraction at 2.0 Å resolution. Released 11 Jun 2025.
- Method
- X-ray diffraction
- Resolution
- 2.0 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 8,486
- Mol. weight
- 116.45 kDa
- Released
- 11 Jun 2025
Explore 9DL0 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9DL0 contains 45 α-helices and 86 β-strands across 6 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 A: 9 helices, 22 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 6-10 | 5 | 1 |
| β-strand | 13-15 | 3 | 2 |
| β-strand | 21-28 | 8 | 1 |
| α-helix | 32-34 | 3 | |
| β-strand | 36-42 | 7 | 2 |
| β-strand | 49-55 | 7 | 2 |
| β-strand | 61-63 | 3 | 2 |
| β-strand | 71-76 | 6 | 1 |
| α-helix | 77-79 | 3 | |
| β-strand | 81-86 | 6 | 1 |
| α-helix | 91-93 | 3 | |
| β-strand | 95-104 | 10 | 2 |
| β-strand | 111-116 | 6 | 2 |
| β-strand | 120-124 | 5 | 2 |
| α-helix | 128-129 | 2 | |
| β-strand | 130 | 1 | 3 |
| α-helix | 131-132 | 2 | |
| β-strand | 133-137 | 5 | 4 |
| β-strand | 148-158 | 11 | 4 |
| β-strand | 159 | 1 | 3 |
| β-strand | 164-167 | 4 | 5 |
| α-helix | 168-170 | 3 | |
| β-strand | 172 | 1 | 5 |
| β-strand | 176-178 | 3 | 4 |
| α-helix | 179-181 | 3 | |
| β-strand | 182-183 | 2 | 4 |
| β-strand | 189-198 | 10 | 4 |
| α-helix | 199-201 | 3 | |
| β-strand | 207-213 | 7 | 5 |
| α-helix | 214-216 | 3 | |
| β-strand | 218-224 | 7 | 5 |
Chain G: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2023-2035 | 13 | |
| α-helix | 2036-2040 | 5 | |
| α-helix | 2044-2060 | 17 | |
| α-helix | 2065-2091 | 27 | |
| α-helix | 2094-2111 | 18 | |
Chain H: 9 helices, 22 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 6-10 | 5 | 6 |
| β-strand | 13-15 | 3 | 7 |
| β-strand | 21-28 | 8 | 6 |
| α-helix | 32-34 | 3 | |
| β-strand | 36-42 | 7 | 7 |
| β-strand | 48-55 | 8 | 7 |
| β-strand | 61-63 | 3 | 7 |
| β-strand | 71-76 | 6 | 6 |
| α-helix | 77-79 | 3 | |
| β-strand | 81-86 | 6 | 6 |
| α-helix | 91-93 | 3 | |
| β-strand | 95-104 | 10 | 7 |
| β-strand | 111-116 | 6 | 7 |
| β-strand | 120-124 | 5 | 7 |
| α-helix | 128-129 | 2 | |
| β-strand | 130 | 1 | 8 |
| α-helix | 131-132 | 2 | |
| β-strand | 133-137 | 5 | 9 |
| β-strand | 148-158 | 11 | 9 |
| β-strand | 159 | 1 | 8 |
| β-strand | 164-167 | 4 | 10 |
| α-helix | 168-170 | 3 | |
| β-strand | 172 | 1 | 10 |
| β-strand | 176-178 | 3 | 9 |
| α-helix | 179-181 | 3 | |
| β-strand | 182-183 | 2 | 9 |
| β-strand | 189-198 | 10 | 9 |
| α-helix | 199-201 | 3 | |
| β-strand | 207-213 | 7 | 10 |
| α-helix | 214-216 | 3 | |
| β-strand | 218-224 | 7 | 10 |
Chain I: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2023-2035 | 13 | |
| α-helix | 2036-2040 | 5 | |
| α-helix | 2044-2059 | 16 | |
| α-helix | 2065-2091 | 27 | |
| α-helix | 2094-2114 | 21 | |
Chain Y: 9 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-8 | 4 | 11 |
| β-strand | 11-15 | 5 | 12 |
| β-strand | 20-26 | 7 | 11 |
| β-strand | 34-39 | 6 | 12 |
| β-strand | 46-50 | 5 | 12 |
| β-strand | 54-55 | 2 | 12 |
| α-helix | 56 | 1 | |
| β-strand | 63-68 | 6 | 11 |
| β-strand | 71-76 | 6 | 11 |
| α-helix | 81-83 | 3 | |
| β-strand | 85-91 | 7 | 12 |
| α-helix | 97 | 1 | |
| β-strand | 98-99 | 2 | 12 |
| β-strand | 103-108 | 6 | 12 |
| β-strand | 112 | 1 | 13 |
| α-helix | 113-114 | 2 | |
| β-strand | 115-119 | 5 | 14 |
| α-helix | 120-122 | 3 | |
| α-helix | 123-126 | 4 | |
| β-strand | 130-140 | 11 | 14 |
| β-strand | 141 | 1 | 13 |
| β-strand | 146-151 | 6 | 15 |
| β-strand | 154-155 | 2 | 15 |
| α-helix | 156 | 1 | |
| β-strand | 160-164 | 5 | 14 |
| α-helix | 165-168 | 4 | |
| β-strand | 174-183 | 10 | 14 |
| α-helix | 184-188 | 5 | |
| β-strand | 192-198 | 7 | 15 |
| β-strand | 206-211 | 6 | 15 |
Chain Z: 8 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-8 | 4 | 16 |
| β-strand | 11-15 | 5 | 17 |
| β-strand | 20-26 | 7 | 16 |
| β-strand | 34-39 | 6 | 17 |
| β-strand | 46-50 | 5 | 17 |
| β-strand | 54-55 | 2 | 17 |
| α-helix | 56 | 1 | |
| β-strand | 63-68 | 6 | 16 |
| β-strand | 71-76 | 6 | 16 |
| α-helix | 81-83 | 3 | |
| β-strand | 85-91 | 7 | 17 |
| β-strand | 98-99 | 2 | 17 |
| β-strand | 103-108 | 6 | 17 |
| β-strand | 112 | 1 | 18 |
| α-helix | 113-114 | 2 | |
| β-strand | 115-119 | 5 | 19 |
| α-helix | 120-122 | 3 | |
| α-helix | 123-126 | 4 | |
| β-strand | 130-140 | 11 | 19 |
| β-strand | 141 | 1 | 18 |
| β-strand | 146-151 | 6 | 20 |
| β-strand | 154-155 | 2 | 20 |
| α-helix | 156 | 1 | |
| β-strand | 160-164 | 5 | 19 |
| α-helix | 165-168 | 4 | |
| β-strand | 174-183 | 10 | 19 |
| α-helix | 184-188 | 5 | |
| β-strand | 192-198 | 7 | 20 |
| β-strand | 206-211 | 6 | 20 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Fab heavy chain | A, H | protein | 224 | Homo sapiens | |
| Serine/threonine-protein kinase mTOR | G, I | protein | 98 | Homo sapiens | P42345 (AlphaFold model) |
| Fab light chain | Y, Z | protein | 212 | Homo sapiens | |
Sequence of entity 1 (A, H), FASTA
>9DL0_1 Fab heavy chain (chains A, H)
EVQLVESGGGLVQPGGSLRLSCAASGFNFSSSYIHWVRQAPGKGLEWVASISSSSGSTSY
ADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARFSYMSGSVFWALDYWGQGTLVT
VSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVL
QSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPK
Sequence of entity 2 (G, I), FASTA
>9DL0_2 Serine/threonine-protein kinase mTOR (chains G, I)
SILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRDLM
EAQEWCRKYMKSGNVKDLTQAWDLYYHVFRRISKGGGG
Sequence of entity 3 (Y, Z), FASTA
>9DL0_3 Fab light chain (chains Y, Z)
DIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVPS
RFSGSRSGTDFTLTISSLQPEDFATYYCQQSSWFPITFGQGTKVEIKRTVAAPSVFIFPP
SDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT
LSKADYEKHKVYACEVTHQGLSSPVTKSFNRG
Primary citation
Conformation-specific synthetic intrabodies modulate mTOR signaling with subcellular spatial resolution. O'Leary, K.M., Slezak, T., Kossiakoff, A.A. Proc Natl Acad Sci U S A (2025) 122:e2424679122-e2424679122. DOI 10.1073/pnas.2424679122 · PubMed
Other PDB entries of the same protein (UniProt P42345 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 4DRI 1.45 Å, Co-crystal structure of the PPIase domain of FKBP51, Rapamycin and the FRB fragment of…
- 9DBO 1.55 Å, Crystal structure of a synthetic Fab (R3E9) in complex with the FRB domain of mTOR
- 5GPG 1.67 Å, Co-crystal structure of the FK506 binding domain of human FKBP25, Rapamycin and the FRB…
- 5WBH 1.75 Å, Structure of the FRB domain of mTOR bound to a substrate recruitment peptide of S6K1
- 4DRJ 1.8 Å, o-crystal structure of the PPIase domain of FKBP52, Rapamycin and the FRB fragment of mTOR
- 3FAP 1.85 Å, Atomic structures of the rapamycin analogs in complex with both human FKBP12 and frb…
- 8PPZ 1.85 Å, Co-crystal structure of FKBP12, compound 7 and the FRB fragment of mTOR
- 8XI9 1.85 Å, Crystal structure of FRB-FKBP fusion protein in complex with rapamycin
- 9PIW 1.9 Å, Crystal structure of a synthetic Fab (1A) in complex with the FRB domain of mTOR
- 9PJ1 2.05 Å, Crystal structure of a synthetic Fab (4R) in complex with the ternary assembly of…
- 9PIU 2.18 Å, Crystal structure of a synthetic Fab (2C) in complex with the FRB domain of mTOR
- 1NSG 2.2 Å, The structure of the immunophilin-immunosuppressant FKBP12-rapamycin complex interacting…
Browse structure collections
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