Download MendeleyThe 0.98 angstrom structure of the human FABP3 Y19F mutant complexed with palmitic acid
Sugiyama, S., Takahashi, J., Matsuoka, S., Tsuchikawa, H., Sonoyama, M., Inoue, Y., Hayashi, F., Murata, M.To be published.
7V2G
The 0.98 angstrom structure of the human FABP3 Y19F mutant complexed with palmitic acid
- PDB DOI: https://doi.org/10.2210/pdb7V2G/pdb
- Classification: LIPID BINDING PROTEIN
- Organism(s): Homo sapiens
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2021-08-09 Released: 2022-08-10
- Funding Organization(s): Japan Science and Technology, Japan Society for the Promotion of Science (JSPS), Other private
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 0.98 Å
- R-Value Free: 0.117
- R-Value Work: 0.101
- R-Value Observed: 0.102
Starting Model: experimental
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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 |
| Fatty acid-binding protein, heart | 133 | Homo sapiens | Mutation(s): 1 Gene Names: FABP3, FABP11, MDGI |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P05413 (Homo sapiens) Explore P05413 Go to UniProtKB: P05413 | |||||
PHAROS: P05413 GTEx: ENSG00000121769 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P05413 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| P6G (Subject of Investigation/LOI) Query on P6G | C [auth A], D [auth A] | HEXAETHYLENE GLYCOL C12 H26 O7 IIRDTKBZINWQAW-UHFFFAOYSA-N |  | ||
| PLM (Subject of Investigation/LOI) Query on PLM | B [auth A] | PALMITIC ACID C16 H32 O2 IPCSVZSSVZVIGE-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 0.98 Å
- R-Value Free: 0.117
- R-Value Work: 0.101
- R-Value Observed: 0.102
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 54.588 | α = 90 |
| b = 69.726 | β = 90 |
| c = 33.938 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| MOLREP | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2022-08-10 Deposition Author(s): Sugiyama, S., Takahashi, J., Matsuoka, S., Tsuchikawa, H., Sonoyama, M., Inoue, Y., Hayashi, F., Murata, M.
| Funding Organization | Location | Grant Number |
|---|---|---|
| Japan Science and Technology | Japan | JPMJTM19DC |
| Japan Science and Technology | Japan | JPMJER1005 |
| Japan Society for the Promotion of Science (JSPS) | Japan | 19K06588 |
| Other private | Japan | 09-003-005 |
Revision History (Full details and data files)
- Version 1.0: 2022-08-10
Type: Initial release - Version 1.1: 2023-11-29
Changes: Data collection, Refinement description
