8ER6: FKBP12-FRB
FKBP12-FRB in Complex with Compound 11. Determined by X-ray diffraction at 2.81 Å resolution. Released 28 Dec 2022.
- Method
- X-ray diffraction
- Resolution
- 2.81 Å
- Organism
- Homo sapiens
- Chains
- 6
- Atoms
- 5,146
- Mol. weight
- 72.49 kDa
- Ligands
- XYU
- Released
- 28 Dec 2022
Explore 8ER6 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8ER6 contains 39 α-helices and 24 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: 7 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-9 | 7 | 1 |
| α-helix | 16-18 | 3 | |
| β-strand | 22-31 | 10 | 1 |
| β-strand | 36-39 | 4 | 1 |
| α-helix | 40-43 | 4 | |
| α-helix | 46 | 1 | |
| β-strand | 47-50 | 4 | 1 |
| α-helix | 58-63 | 6 | |
| α-helix | 64-66 | 3 | |
| α-helix | 67-68 | 2 | |
| β-strand | 72-77 | 6 | 1 |
| α-helix | 79-81 | 3 | |
| β-strand | 88 | 1 | 2 |
| β-strand | 92 | 1 | 2 |
| β-strand | 98-107 | 10 | 1 |
Chain B: 6 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2023-2035 | 13 | |
| α-helix | 2036-2040 | 5 | |
| α-helix | 2041 | 1 | |
| α-helix | 2044-2060 | 17 | |
| α-helix | 2065-2091 | 27 | |
| α-helix | 2094-2111 | 18 | |
Chain C: 6 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-9 | 7 | 3 |
| α-helix | 16-18 | 3 | |
| β-strand | 22-31 | 10 | 3 |
| β-strand | 36-39 | 4 | 3 |
| α-helix | 40-43 | 4 | |
| α-helix | 46 | 1 | |
| β-strand | 47-50 | 4 | 3 |
| α-helix | 58-65 | 8 | |
| α-helix | 67-68 | 2 | |
| β-strand | 72-77 | 6 | 3 |
| α-helix | 79-81 | 3 | |
| β-strand | 88 | 1 | 4 |
| β-strand | 92 | 1 | 4 |
| β-strand | 98-107 | 10 | 3 |
Chain D: 6 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2023-2035 | 13 | |
| α-helix | 2036-2040 | 5 | |
| α-helix | 2041 | 1 | |
| α-helix | 2044-2058 | 15 | |
| α-helix | 2065-2091 | 27 | |
| α-helix | 2094-2111 | 18 | |
Chain E: 8 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-9 | 7 | 5 |
| α-helix | 16-18 | 3 | |
| α-helix | 21 | 1 | |
| β-strand | 22-31 | 10 | 5 |
| β-strand | 36-39 | 4 | 5 |
| α-helix | 40-43 | 4 | |
| α-helix | 46 | 1 | |
| β-strand | 47-50 | 4 | 5 |
| α-helix | 58-63 | 6 | |
| α-helix | 64-66 | 3 | |
| α-helix | 67-68 | 2 | |
| β-strand | 72-77 | 6 | 5 |
| α-helix | 79-81 | 3 | |
| β-strand | 88 | 1 | 6 |
| β-strand | 92 | 1 | 6 |
| β-strand | 98-107 | 10 | 5 |
Chain F: 6 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2023-2035 | 13 | |
| α-helix | 2036-2040 | 5 | |
| α-helix | 2041 | 1 | |
| α-helix | 2044-2060 | 17 | |
| α-helix | 2065-2091 | 27 | |
| α-helix | 2095-2111 | 17 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Peptidyl-prolyl cis-trans isomerase FKBP1A | A, C, E | protein | 107 | Homo sapiens | P62942 (AlphaFold model) |
| non-specific serine/threonine protein kinase | B, D, F | protein | 95 | Homo sapiens | P42345 (AlphaFold model) |
Sequence of entity 1 (A, C, E), FASTA
>8ER6_1 Peptidyl-prolyl cis-trans isomerase FKBP1A (chains A, C, E)
GVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFMLGKQEVIRGWE
EGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPHATLVFDVELLKLE
Sequence of entity 2 (B, D, F), FASTA
>8ER6_2 non-specific serine/threonine protein kinase (chains B, D, F)
GVAILWHEMWHEGLEEASRLYFGERNVKGMFEVLEPLHAMMERGPQTLKETSFNQAYGRD
LMEAQEWCRKYMKSGNVKDLTQAWDLYYHVFRRIS
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| XYU | (3S,5R,6R,7E,9R,10R,12R,14S,15E,17E,19E,21S,23S,26R,27R,30R,34aS)-5,9,27-trihyd… | C51 H81 N O13 | 3 |
Water and common crystallization additives (EDO) are not listed.
Primary citation
Discovery of RMC-5552, a Selective Bi-Steric Inhibitor of mTORC1, for the Treatment of mTORC1-Activated Tumors. Burnett, G.L., Yang, Y.C., Aggen, J.B. et al. J Med Chem (2023) 66:149-169. DOI 10.1021/acs.jmedchem.2c01658 · PubMed
Other PDB entries of the same protein (UniProt P62942 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 2PPN 0.92 Å, Crystal structure of FKBP12
- 2PPP 0.94 Å, Crystal structure of E60Q mutant of FKBP12
- 6YF3 1.0 Å, FKBP12 in complex with the BMP potentiator compound 10 at 1.00A resolution
- 6YF2 1.03 Å, FKBP12 in complex with the BMP potentiator compound 6 at 1.03A resolution
- 8X6P 1.05 Å, Isomerase Protein
- 6YF1 1.12 Å, FKBP12 in complex with the BMP potentiator compound 8 at 1.12A resolution
- 8CHM 1.12 Å, Human FKBP12 in complex with (1S,5S,6R)-10-((S)-(3,5-dichlorophenyl)sulfinyl)-3-(pyridin-…
- 4N19 1.2 Å, Structural basis of conformational transitions in the active site and 80 s loop in the…
- 8PDF 1.2 Å, FKBP12 in complex with PROTAC 6a2
- 9LYG 1.26 Å, Crystal structure of FKBP12 complexed with Small Molecule Anchor for Protein-201
- 2PPO 1.29 Å, Crystal structure of E60A mutant of FKBP12
- 7U8D 1.39 Å, FKBP12 mutant V55G bound to Rapa*-3Z
Browse structure collections
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