Download MendeleyPhotoswitching fluorescence via a novel Trp-flap mechanism
Bingham, C., Maity, S., Ehyaei, N., Cantrell, J., Gwasdacus, J., Sheng, W., Vasileiou, C., Borhan, B., Geiger, J.H.To be published.
9D8M | pdb_00009d8m
Q108K:K40L:T51V:T53C:R58W:Y19W:Q38L:Q4A:T29L mutant of hCRBPII bound to FR1V fluorophore in the dark state at pH 4
- PDB DOI: https://doi.org/10.2210/pdb9D8M/pdb
- Classification: RETINOL BINDING PROTEIN
- Organism(s): Homo sapiens
- Expression System: Escherichia coli
- Mutation(s): Yes
- Deposited: 2024-08-19 Released: 2025-02-12
- Funding Organization(s): National Institutes of Health/National Institute of Biomedical Imaging and Bioengineering (NIH/NIBIB)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.20 Å
- R-Value Free: 0.204 (Depositor), 0.202 (DCC)
- R-Value Work: 0.193 (Depositor), 0.193 (DCC)
Starting Model: experimental
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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 |
| Retinol-binding protein 2 | 133 | Homo sapiens | Mutation(s): 9 Gene Names: RBP2, CRBP2 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P50120 (Homo sapiens) Explore P50120 Go to UniProtKB: P50120 | |||||
PHAROS: P50120 GTEx: ENSG00000114113 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P50120 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| ZFJ (Subject of Investigation/LOI) Query on ZFJ | C [auth A], E [auth B] | (4aP)-N,N-diethyl-9,9-dimethyl-7-[(1E)-prop-1-en-1-yl]-9H-fluoren-2-amine C22 H27 N UMARKYXLRJLTSK-RMKNXTFCSA-N |  | ||
| ACY Query on ACY | D [auth A], F [auth B] | ACETIC ACID C2 H4 O2 QTBSBXVTEAMEQO-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.20 Å
- R-Value Free: 0.204 (Depositor), 0.202 (DCC)
- R-Value Work: 0.193 (Depositor), 0.193 (DCC)
Space Group: P 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 31.171 | α = 85.66 |
| b = 35.859 | β = 86.04 |
| c = 64.046 | γ = 65.17 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
| PHENIX | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2025-02-12 Deposition Author(s): Ehyaei, N., Bingham, C., Geiger, J.H.
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Institutes of Health/National Institute of Biomedical Imaging and Bioengineering (NIH/NIBIB) | United States | -- |
Revision History (Full details and data files)
- Version 1.0: 2025-02-12
Type: Initial release
