Download MendeleyThe anabolic steroid stanozolol is a potent inhibitor of human MutT homolog 1
Scaletti Hutchinson, E., Gustafsson Westergren, R., Almlof, I., Jemth, A.S., Scobie, M., Warpman Berglund, U., Helleday, T., Stenmark, P.(2025) FEBS Lett n/a
9GQL | pdb_00009gql
Human MTH1 in complex with stanozolol
- PDB DOI: https://doi.org/10.2210/pdb9GQL/pdb
- Classification: HYDROLASE
- Organism(s): Homo sapiens
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2024-09-09 Released: 2025-08-13
- Funding Organization(s): Cancerfonden
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.40 Å
- R-Value Free: 0.192 (Depositor), 0.194 (DCC)
- R-Value Work: 0.148 (Depositor), 0.153 (DCC)
Starting Model: experimental
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This is version 1.0 of the entry. See complete history.
Literature
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Oxidized purine nucleoside triphosphate hydrolase | 156 | Homo sapiens | Mutation(s): 0 Gene Names: NUDT1, MTH1 EC: 3.6.1.56 (PDB Primary Data), 3.6.1 (PDB Primary Data) |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P36639 (Homo sapiens) Explore P36639 Go to UniProtKB: P36639 | |||||
PHAROS: P36639 GTEx: ENSG00000106268 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P36639 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| A1IOS (Subject of Investigation/LOI) Query on A1IOS | B [auth A] | stanozolol C21 H32 N2 O LKAJKIOFIWVMDJ-IYRCEVNGSA-N |  | ||
| SO4 Query on SO4 | D [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| GOL Query on GOL | C [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.40 Å
- R-Value Free: 0.192 (Depositor), 0.194 (DCC)
- R-Value Work: 0.148 (Depositor), 0.153 (DCC)
Space Group: P 2 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 36.526 | α = 90 |
| b = 59.71 | β = 90 |
| c = 66.875 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| XDS | data reduction |
| Aimless | data scaling |
| PHASER | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2025-08-13 Deposition Author(s): Scaletti Hutchinson, E., Gustafsson Westergren, R., Stenmark, P.
| Funding Organization | Location | Grant Number |
|---|---|---|
| Cancerfonden | Sweden | -- |
Revision History (Full details and data files)
- Version 1.0: 2025-08-13
Type: Initial release
