9TRU: Zebrafish dUTPase
Zebrafish dUTPase in complex with staphylococcal Stl repressor. Determined by X-ray diffraction at 2.26 Å resolution. Released 23 Sept 2026.
- Method
- X-ray diffraction
- Resolution
- 2.26 Å
- Organisms
- Danio rerio, Staphylococcus aureus
- Chains
- 12
- Atoms
- 13,671
- Mol. weight
- 229.74 kDa
- Ligands
- MG
- Released
- 23 Sept 2026
Explore 9TRU in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9TRU contains 99 α-helices and 87 β-strands across 12 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: 5 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 26-31 | 6 | 1 |
| β-strand | 40 | 1 | 2 |
| β-strand | 49-52 | 4 | 2 |
| β-strand | 57-59 | 3 | 3 |
| α-helix | 60 | 1 | |
| β-strand | 63-68 | 6 | 4 |
| β-strand | 71-74 | 4 | 1 |
| α-helix | 75-76 | 2 | |
| β-strand | 79-84 | 6 | 2 |
| α-helix | 87-93 | 7 | |
| β-strand | 95-98 | 4 | 4 |
| β-strand | 101-102 | 2 | 2 |
| β-strand | 111-116 | 6 | 4 |
| β-strand | 122-124 | 3 | 3 |
| β-strand | 129-137 | 9 | 2 |
| β-strand | 138 | 1 | 5 |
| α-helix | 141 | 1 | |
| β-strand | 142-146 | 5 | 6 |
| α-helix | 149-152 | 4 | |
Chain B: 4 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 26-31 | 6 | 7 |
| β-strand | 40 | 1 | 8 |
| β-strand | 48-52 | 5 | 8 |
| β-strand | 57-59 | 3 | 9 |
| α-helix | 60 | 1 | |
| β-strand | 63-68 | 6 | 10 |
| β-strand | 71-74 | 4 | 7 |
| α-helix | 75-76 | 2 | |
| β-strand | 79-84 | 6 | 8 |
| α-helix | 87-93 | 7 | |
| β-strand | 95-98 | 4 | 10 |
| β-strand | 101-102 | 2 | 8 |
| β-strand | 111-116 | 6 | 10 |
| β-strand | 122-124 | 3 | 9 |
| β-strand | 129-137 | 9 | 8 |
| β-strand | 138 | 1 | 2 |
| α-helix | 141 | 1 | |
| β-strand | 142-145 | 4 | 1 |
Chain C: 4 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 26-31 | 6 | 6 |
| β-strand | 40 | 1 | 5 |
| β-strand | 49-52 | 4 | 5 |
| β-strand | 57-59 | 3 | 11 |
| α-helix | 60 | 1 | |
| β-strand | 63-68 | 6 | 12 |
| β-strand | 71-74 | 4 | 6 |
| α-helix | 75-76 | 2 | |
| β-strand | 79-84 | 6 | 5 |
| α-helix | 87-93 | 7 | |
| β-strand | 95-98 | 4 | 12 |
| β-strand | 101-102 | 2 | 5 |
| β-strand | 111-116 | 6 | 12 |
| β-strand | 122-124 | 3 | 11 |
| β-strand | 129-137 | 9 | 5 |
| β-strand | 138 | 1 | 8 |
| α-helix | 141 | 1 | |
| β-strand | 142-146 | 5 | 7 |
Chains D and F: 5 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 26-31 | 6 | 13 |
| β-strand | 40 | 1 | 14 |
| β-strand | 48-52 | 5 | 14 |
| β-strand | 57-59 | 3 | 15 |
| α-helix | 60 | 1 | |
| β-strand | 63-68 | 6 | 16 |
| β-strand | 71-74 | 4 | 13 |
| α-helix | 75-76 | 2 | |
| β-strand | 79-84 | 6 | 14 |
| α-helix | 87-93 | 7 | |
| β-strand | 95-98 | 4 | 16 |
| β-strand | 101-102 | 2 | 14 |
| β-strand | 111-116 | 6 | 16 |
| β-strand | 122-124 | 3 | 15 |
| β-strand | 129-137 | 9 | 14 |
| β-strand | 138 | 1 | 17 |
| α-helix | 141 | 1 | |
| β-strand | 142-145 | 4 | 18 |
| α-helix | 149-151 | 3 | |
Chain E: 4 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 26-31 | 6 | 19 |
| β-strand | 40 | 1 | 20 |
| β-strand | 49-52 | 4 | 20 |
| β-strand | 57-59 | 3 | 21 |
| α-helix | 60 | 1 | |
| β-strand | 63-68 | 6 | 22 |
| β-strand | 71-74 | 4 | 19 |
| α-helix | 75-76 | 2 | |
| β-strand | 79-84 | 6 | 20 |
| α-helix | 87-93 | 7 | |
| β-strand | 95-98 | 4 | 22 |
| β-strand | 101-102 | 2 | 20 |
| β-strand | 111-116 | 6 | 22 |
| β-strand | 122-124 | 3 | 21 |
| β-strand | 129-137 | 9 | 20 |
| β-strand | 138 | 1 | 14 |
| α-helix | 141 | 1 | |
| β-strand | 142-145 | 4 | 13 |
Chain G: 12 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 13-24 | 12 | |
| α-helix | 29-36 | 8 | |
| α-helix | 40-47 | 8 | |
| α-helix | 52-54 | 3 | |
| α-helix | 57-65 | 9 | |
| α-helix | 69-82 | 14 | |
| β-strand | 84 | 1 | 9 |
| α-helix | 86-89 | 4 | |
| α-helix | 91-107 | 17 | |
| α-helix | 109-112 | 4 | |
| α-helix | 118-131 | 14 | |
| α-helix | 136-138 | 3 | |
| α-helix | 141-152 | 12 | |
Chain H: 12 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 9 | 1 | 25 |
| α-helix | 13-24 | 12 | |
| α-helix | 29-36 | 8 | |
| α-helix | 40-47 | 8 | |
| α-helix | 52-53 | 2 | |
| β-strand | 54 | 1 | 25 |
| α-helix | 57-65 | 9 | |
| α-helix | 69-82 | 14 | |
| α-helix | 86-89 | 4 | |
| α-helix | 91-107 | 17 | |
| α-helix | 109-112 | 4 | |
| α-helix | 118-131 | 14 | |
| α-helix | 136-138 | 3 | |
| α-helix | 141-152 | 12 | |
Chain I: 12 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 13-24 | 12 | |
| α-helix | 29-36 | 8 | |
| α-helix | 40-47 | 8 | |
| α-helix | 52-54 | 3 | |
| α-helix | 57-65 | 9 | |
| α-helix | 69-82 | 14 | |
| α-helix | 86-89 | 4 | |
| α-helix | 91-107 | 17 | |
| α-helix | 109-112 | 4 | |
| α-helix | 118-132 | 15 | |
| α-helix | 136-138 | 3 | |
| α-helix | 141-152 | 12 | |
2 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Deoxyuridine 5'-triphosphate nucleotidohydrolase | A, B, C, D, E, F | protein | 186 | Danio rerio | Q5XJ23 (AlphaFold model) |
| Orf20 | G, H, I, J, K, L | protein | 156 | Staphylococcus aureus | Q9F0J8 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>9TRU_1 Deoxyuridine 5'-triphosphate nucleotidohydrolase (chains A, B, C, D, E, F)
MGSSHHHHHHSSGLVPRGSHMSEVTEAVSPHKRAKSDAVNGAEERAVLKFAKLTEHATTP
SRGSNRAAGYDLYSAYDYSIGPMDKTLVKTGIQIAVPHGYYGRVAPRSGLAVKHFVDVGA
GVVDEDYRGNLGVVIFNFNKEPFEVKKGDRIAQLICEKICYPDLQELQTLDETERGAGGF
GSTGTN
Sequence of entity 2 (G, H, I, J, K, L), FASTA
>9TRU_2 Orf20 (chains G, H, I, J, K, L)
MEGAGQMAELPTHYGTIIKTLRKYMKLTQSKLSERTGFSQNTISNHENGNRNIGVNEIEI
YGKGLGIPSYILHRISDEFKEKGYSPTLNDFGKFDKMYSYVNKAYYNDGDIYYSSYDLYD
ETIKLLELLKESKINVNDIDYDYVLKLYKQILSTDT
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| MG | Magnesium ion | Mg | 2 |
Primary citation
A bacterial protein inhibitor of dUTPase disrupts zebrafish embryogenesis through a conserved active-site mechanism. Perey-Simon, V., Toth, Z.S., Dombovari, D. et al. Protein Sci (2026) 35:e70767-e70767. DOI 10.1002/pro.70767 · PubMed
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