Download MendeleyStructural and Mechanistic Basis of Substrate Recognition by Novel Di-peptidase Dug1p From Saccromyces cerevesiae
Singh, A.K., Singh, M., Pandya, V.K., Singh, V., Mittal, M., Kumaran, S.To be published.
4G1P | pdb_00004g1p
Structural and Mechanistic Basis of Substrate Recognition by Novel Di-peptidase Dug1p From Saccharomyces cerevisiae
- PDB DOI: https://doi.org/10.2210/pdb4G1P/pdb
- Classification: HYDROLASE
- Organism(s): Saccharomyces cerevisiae S288C
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2012-07-11 Released: 2013-07-17
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.55 Å
- R-Value Free: 0.231 (Depositor), 0.230 (DCC)
- R-Value Work: 0.186 (Depositor), 0.190 (DCC)
- R-Value Observed: 0.188 (Depositor)
Starting Model: experimental
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wwPDB Validation 3D Report Full Report
This is version 1.2 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 |
| Cys-Gly metallodipeptidase DUG1 | 487 | Saccharomyces cerevisiae S288C | Mutation(s): 0 Gene Names: Dug1p EC: 3.4.13 |  | |
UniProt | |||||
Find proteins for P43616 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c)) Explore P43616 Go to UniProtKB: P43616 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P43616 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| CYS Query on CYS | E [auth A] | CYSTEINE C3 H7 N O2 S XUJNEKJLAYXESH-REOHCLBHSA-N |  | ||
| GLY Query on GLY | D [auth A] | GLYCINE C2 H5 N O2 DHMQDGOQFOQNFH-UHFFFAOYSA-N |  | ||
| ZN Query on ZN | B [auth A], C [auth A] | ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.55 Å
- R-Value Free: 0.231 (Depositor), 0.230 (DCC)
- R-Value Work: 0.186 (Depositor), 0.190 (DCC)
- R-Value Observed: 0.188 (Depositor)
Space Group: P 65 2 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 119.132 | α = 90 |
| b = 119.132 | β = 90 |
| c = 176.302 | γ = 120 |
| Software Name | Purpose |
|---|---|
| MAR345dtb | data collection |
| PHASES | phasing |
| PHENIX | refinement |
| XDS | data reduction |
| XDS | data scaling |
Entry History
Deposition Data
- Released Date: 2013-07-17 Deposition Author(s): Singh, A.K., Singh, M., Pandya, V.K., Singh, V., Mittal, M., Kumaran, S.
Revision History (Full details and data files)
- Version 1.0: 2013-07-17
Type: Initial release - Version 1.1: 2014-09-17
Changes: Other - Version 1.2: 2023-11-08
Changes: Data collection, Database references, Derived calculations, Refinement description
