6C4U: Engineered FHA with Myc-pTBD peptide
Engineered FHA with Myc-pTBD peptide. Determined by X-ray diffraction at 2.6 Å resolution. Released 30 May 2018.
- Method
- X-ray diffraction
- Resolution
- 2.6 Å
- Organisms
- Saccharomyces cerevisiae, Homo sapiens
- Chains
- 12
- Atoms
- 6,481
- Mol. weight
- 97.17 kDa
- Released
- 30 May 2018
Explore 6C4U in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6C4U contains 27 α-helices and 66 β-strands across 9 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: 4 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 32-38 | 7 | 9 |
| β-strand | 45-49 | 5 | 9 |
| α-helix | 52-57 | 6 | |
| β-strand | 62-69 | 8 | 10 |
| β-strand | 76-77 | 2 | 10 |
| β-strand | 89-94 | 6 | 10 |
| β-strand | 99-103 | 5 | 10 |
| β-strand | 109-111 | 3 | 9 |
| β-strand | 114-115 | 2 | 9 |
| α-helix | 116-117 | 2 | |
| β-strand | 122-124 | 3 | 10 |
| α-helix | 125 | 1 | |
| β-strand | 129-133 | 5 | 9 |
| β-strand | 140-147 | 8 | 9 |
| α-helix | 149-153 | 5 | |
Chain B: 4 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 32-38 | 7 | 1 |
| β-strand | 45-49 | 5 | 1 |
| α-helix | 52-57 | 6 | |
| β-strand | 62-69 | 8 | 2 |
| β-strand | 76-77 | 2 | 2 |
| β-strand | 89-94 | 6 | 2 |
| β-strand | 99-103 | 5 | 2 |
| β-strand | 110-111 | 2 | 1 |
| β-strand | 114-115 | 2 | 1 |
| α-helix | 116-117 | 2 | |
| β-strand | 122-123 | 2 | 2 |
| α-helix | 124-125 | 2 | |
| β-strand | 129-133 | 5 | 1 |
| β-strand | 140-147 | 8 | 1 |
| α-helix | 149-153 | 5 | |
Chains C and E: 4 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 32-38 | 7 | 3 |
| β-strand | 45-49 | 5 | 3 |
| α-helix | 52-57 | 6 | |
| β-strand | 62-69 | 8 | 4 |
| β-strand | 76-77 | 2 | 4 |
| β-strand | 89-94 | 6 | 4 |
| β-strand | 99-103 | 5 | 4 |
| β-strand | 109-111 | 3 | 3 |
| β-strand | 114-115 | 2 | 3 |
| α-helix | 116-117 | 2 | |
| β-strand | 122-123 | 2 | 4 |
| α-helix | 124-125 | 2 | |
| β-strand | 129-133 | 5 | 3 |
| β-strand | 140-147 | 8 | 3 |
| α-helix | 149-153 | 5 | |
Chain D: 4 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 32-38 | 7 | 5 |
| β-strand | 45-49 | 5 | 5 |
| α-helix | 52-57 | 6 | |
| β-strand | 62-69 | 8 | 6 |
| β-strand | 76-77 | 2 | 6 |
| β-strand | 89-94 | 6 | 6 |
| β-strand | 99-103 | 5 | 6 |
| β-strand | 110-111 | 2 | 5 |
| β-strand | 114-115 | 2 | 5 |
| α-helix | 116-117 | 2 | |
| β-strand | 122-123 | 2 | 6 |
| α-helix | 124-125 | 2 | |
| β-strand | 129-133 | 5 | 5 |
| β-strand | 139-147 | 9 | 5 |
| α-helix | 149-153 | 5 | |
Chain F: 4 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 32-38 | 7 | 11 |
| β-strand | 46-49 | 4 | 11 |
| α-helix | 52-57 | 6 | |
| β-strand | 62-69 | 8 | 12 |
| β-strand | 76-77 | 2 | 12 |
| β-strand | 89-94 | 6 | 12 |
| β-strand | 99-103 | 5 | 12 |
| β-strand | 110-111 | 2 | 11 |
| β-strand | 114-115 | 2 | 11 |
| α-helix | 116-117 | 2 | |
| β-strand | 122-124 | 3 | 12 |
| α-helix | 125 | 1 | |
| β-strand | 129-133 | 5 | 11 |
| β-strand | 140-147 | 8 | 11 |
| α-helix | 149-153 | 5 | |
Chains H and I: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-7 | 3 | |
Chain J: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 3-7 | 5 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Forkhead-associated 1 | A, B, C, D, E, F | protein | 134 | Saccharomyces cerevisiae | P22216 (AlphaFold model) |
| Myc-pTBD peptide | G, H, I, J, K, L | protein | 9 | Homo sapiens | P01106 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>6C4U_1 Forkhead-associated 1 (chains A, B, C, D, E, F)
GENIVFRVISTTGQIPIRDFSADISQVLKEKRSIKKVWTFGRNPACDYHLGNILPVSNKH
FQILLGEDGNLLLNDISTNGTWLNGQKVEKNSYQLLSQGDEITVRTDPTGTILSLVIFIN
DKFKQSLEQNKVDR
Sequence of entity 2 (G, H, I, J, K, L), FASTA
>6C4U_2 Myc-pTBD peptide (chains G, H, I, J, K, L)
KLLPTPPLS
Primary citation
Generating a recombinant phosphothreonine-binding domain for a phosphopeptide of the human transcription factor, c-Myc. Venegas, L.A., Kall, S.L., Bankole, O. et al. N Biotechnol (2018) 45:36-44. DOI 10.1016/j.nbt.2018.05.001 · PubMed
Other PDB entries of the same protein (UniProt P22216 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1G6G 1.6 Å, X-ray structure of the N-terminal fha domain from S. Cerevisiae RAD53P in complex with a…
- 5T2S 2.4 Å, Structure of the FHA1 domain of Rad53 bound simultaneously to the BRCT domain of Dbf4…
- 4PDP 2.59 Å, Crystal structure of Rad53 kinase domain and SCD2
- 5T2F 2.66 Å, Structure of the FHA1 domain of Rad53 bound to the BRCT domain of Dbf4
- 5XZW 2.8 Å, Crystal structure of Rad53 1-466
- 4PDS 2.9 Å, Crystal structure of Rad53 kinase domain and SCD2 in complex with AMPPNP
- 2YGV 2.94 Å, Conserved N-terminal domain of the yeast Histone Chaperone Asf1 in complex with the…
- 5XZV 3.1 Å, Crystal structure of Rad53 1-466 in complex with AMP-PNP
- 1DMZ A refined NMR structure of a new phophopeptide-binding domain containing the FHA2 of RAD53
- 1FHQ Refined solution structure of the FHA2 domain of RAD53
- 1FHR Solution structure of the FHA2 domain of RAD53 complexed with a phosphotyrosyl peptide
- 1G3G NMR structure of the FHA1 domain of yeast RAD53
Browse structure collections
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