Download MendeleyRAMD identification of substrate binding pathways to the active site of dUTPase
Toth, J., Vertessy, B.G., Leveles, I., Bendes, A., Lopata, A.To be published.
4GCY | pdb_00004gcy
Structure of Mycobacterium tuberculosis dUTPase H21W mutant
- PDB DOI: https://doi.org/10.2210/pdb4GCY/pdb
- Classification: HYDROLASE
- Organism(s): Mycobacterium tuberculosis
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): Yes
- Deposited: 2012-07-31 Released: 2013-07-03
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.50 ?
- R-Value Free: 0.158 (Depositor), 0.170 (DCC)
- R-Value Work: 0.123 (Depositor), 0.130 (DCC)
- R-Value Observed: 0.125 (Depositor)
This is version 1.1 of the entry. See complete history.
Literature
To be published.
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Deoxyuridine 5'-triphosphate nucleotidohydrolase | 174 | Mycobacterium tuberculosis | Mutation(s): 1 Gene Names: dut, Rv2697c, MT2771, MTCY05A6.18c EC: 3.6.1.23 |  | |
UniProt | |||||
Find proteins for P9WNS5 (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)) Explore P9WNS5 Go to UniProtKB: P9WNS5 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P9WNS5 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 4 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| DUP Query on DUP | B [auth A] | 2'-DEOXYURIDINE 5'-ALPHA,BETA-IMIDO-TRIPHOSPHATE C9 H16 N3 O13 P3 XZLLMTSKYYYJLH-SHYZEUOFSA-N |  | ||
| TRS Query on TRS | C [auth A] | 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL C4 H12 N O3 LENZDBCJOHFCAS-UHFFFAOYSA-O |  | ||
| GOL Query on GOL | E [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| MG Query on MG | D [auth A] | MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.50 ?
- R-Value Free: 0.158 (Depositor), 0.170 (DCC)
- R-Value Work: 0.123 (Depositor), 0.130 (DCC)
- R-Value Observed: 0.125 (Depositor)
Space Group: P 63
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 54.94 | α = 90 |
| b = 54.94 | β = 90 |
| c = 83.86 | γ = 120 |
| Software Name | Purpose |
|---|---|
| CrystalClear | data collection |
| MOLREP | phasing |
| REFMAC | refinement |
| MOSFLM | data reduction |
| SCALA | data scaling |
Entry History
Deposition Data
- Released Date: 2013-07-03 Deposition Author(s): Toth, J., Vertessy, B.G., Leveles, I., Bendes, A.
Revision History (Full details and data files)
- Version 1.0: 2013-07-03
Type: Initial release - Version 1.1: 2024-02-28
Changes: Data collection, Database references, Derived calculations
