Download MendeleyMultiplexed deconvolution of enzyme function in a PLP-dependent protein family
Zmich, A.P., Perkins, L.J., Bingman, C.A., Buller, A.R.To be published.
8SF4 | pdb_00008sf4
Cystathionine gamma lyase from Thermobifida fusca in internal aldimine form
- PDB DOI: https://doi.org/10.2210/pdb8SF4/pdb
- Classification: LYASE
- Organism(s): Thermobifida fusca
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2023-04-10 Released: 2024-07-03
- Funding Organization(s): National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.46 Å
- R-Value Free: 0.148 (Depositor), 0.150 (DCC)
- R-Value Work: 0.133 (Depositor), 0.130 (DCC)
Starting Model: experimental
View more details
wwPDB Validation 3D Report Full Report
This is version 1.0 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 |
| Cystathionine gamma-lyase | 389 | Thermobifida fusca | Mutation(s): 0 Gene Names: Tfu_0440 EC: 4.4.1.1 |  | |
UniProt | |||||
Find proteins for Q47ST9 (Thermobifida fusca (strain YX)) Explore Q47ST9 Go to UniProtKB: Q47ST9 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q47ST9 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 3 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| 1PE Query on 1PE | C [auth A] | PENTAETHYLENE GLYCOL C10 H22 O6 JLFNLZLINWHATN-UHFFFAOYSA-N |  | ||
| PEG Query on PEG | B [auth A] | DI(HYDROXYETHYL)ETHER C4 H10 O3 MTHSVFCYNBDYFN-UHFFFAOYSA-N |  | ||
| MG Query on MG | D [auth A] | MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| LLP Query on LLP | A | L-PEPTIDE LINKING | C14 H22 N3 O7 P |  | LYS |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.46 Å
- R-Value Free: 0.148 (Depositor), 0.150 (DCC)
- R-Value Work: 0.133 (Depositor), 0.130 (DCC)
Space Group: P 2 3
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 117.591 | α = 90 |
| b = 117.591 | β = 90 |
| c = 117.591 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| XDS | data reduction |
| XSCALE | data scaling |
| PHASER | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2024-07-03 Deposition Author(s): Perkins, L.J., Buller, A.R., Bindman, C.A.
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | United States | 1DP2GM137417-01 |
Revision History (Full details and data files)
- Version 1.0: 2024-07-03
Type: Initial release
