Download MendeleyStructure of the Phosphatidylcholine Binding Mutant of Yeast Sec14 Homolog Sfh1 (S175I,T177I) in Complex with Phosphatidylinositol
Berger, J., Fitz, M., Johnen, P., Shanmugaratnam, S., Hocker, B., Stiel, A.C., Schaaf, G.To be published.
6SLD | pdb_00006sld
Structure of the Phosphatidylcholine Binding Mutant of Yeast Sec14 Homolog Sfh1 (S175I,T177I) in Complex with Phosphatidylinositol
- PDB DOI: https://doi.org/10.2210/pdb6SLD/pdb
- Classification: LIPID TRANSPORT
- Organism(s): Saccharomyces cerevisiae S288C
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2019-08-19 Released: 2020-08-19
- Funding Organization(s): German Research Foundation
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.40 ?
- R-Value Free: 0.164 (Depositor), 0.170 (DCC)
- R-Value Work: 0.143 (Depositor), 0.150 (DCC)
- R-Value Observed: 0.144 (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 |
| CRAL-TRIO domain-containing protein YKL091C | 307 | Saccharomyces cerevisiae S288C | Mutation(s): 2 Gene Names: YKL091C |  | |
UniProt | |||||
Find proteins for P33324 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c)) Explore P33324 Go to UniProtKB: P33324 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P33324 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| B7N (Subject of Investigation/LOI) Query on B7N | B [auth A] | (1R)-2-{[(S)-hydroxy{[(1S,2R,3R,4S,5S,6R)-2,3,4,5,6-pentahydroxycyclohexyl]oxy}phosphoryl]oxy}-1-[(octadecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate C45 H85 O13 P YOBFISPJJWPPTK-BAAZTTAESA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.40 ?
- R-Value Free: 0.164 (Depositor), 0.170 (DCC)
- R-Value Work: 0.143 (Depositor), 0.150 (DCC)
- R-Value Observed: 0.144 (Depositor)
Space Group: P 21 21 21
Unit Cell:
| Length ( ? ) | Angle ( ? ) |
|---|---|
| a = 48.22 | ¦Á = 90 |
| b = 70.81 | ¦Â = 90 |
| c = 90.19 | ¦Ă = 90 |
| Software Name | Purpose |
|---|---|
| XDS | data reduction |
| XSCALE | data scaling |
| PHASER | phasing |
| PHENIX | refinement |
| PDB_EXTRACT | data extraction |
Entry History & Funding Information
Deposition Data
- Released Date: 2020-08-19 Deposition Author(s): Berger, J., Fitz, M., Johnen, P., Shanmugaratnam, S., Hocker, B., Stiel, A.C., Schaaf, G.
| Funding Organization | Location | Grant Number |
|---|---|---|
| German Research Foundation | Germany | Emmy Noether grant 1274/2-1 |
| German Research Foundation | Germany | SCHA 1274/5-1 |
| German Research Foundation | Germany | GRK 2064 |
| German Research Foundation | Germany | Germany's Excellence Strategy, EXC-2070_390732324_PhenoRob |
Revision History (Full details and data files)
- Version 1.0: 2020-08-19
Type: Initial release - Version 1.1: 2024-05-15
Changes: Data collection, Database references
