Download MendeleyCrystal structure of LGR4 fused with hagfish VLR
Xu, J.G., Huang, C., Zhou, Y., Zhu, Y.To be published.
4QXE
Crystal structure of LGR4 fused with hagfish VLR
- PDB DOI: https://doi.org/10.2210/pdb4QXE/pdb
- Classification: MEMBRANE PROTEIN
- Organism(s): Homo sapiens, Eptatretus burgeri
- Expression System: Spodoptera frugiperda
- Mutation(s): Yes
- Deposited: 2014-07-20 Released: 2014-10-22
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 2.20 Å
- R-Value Free: 0.237
- R-Value Work: 0.209
- R-Value Observed: 0.210
This is version 1.3 of the entry. See complete history.
Literature
Macromolecules
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 1 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| Leucine-rich repeat-containing G-protein coupled receptor 4, linker, Variable lymphocyte receptor B | 443 | Homo sapiens, Eptatretus burgeri This entity is chimeric | Mutation(s): 1 Gene Names: GPR48, LGR4, VLRB |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q4G1L2 (Eptatretus burgeri) Explore Q4G1L2 Go to UniProtKB: Q4G1L2 | |||||
Find proteins for Q9BXB1 (Homo sapiens) Explore Q9BXB1 Go to UniProtKB: Q9BXB1 | |||||
PHAROS: Q9BXB1 GTEx: ENSG00000205213 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Groups | Q9BXB1Q4G1L2 | ||||
Sequence AnnotationsExpand | |||||
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Small Molecules
| Ligands 4 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| NAG Query on NAG | B [auth A], C [auth A], D [auth A] | 2-acetamido-2-deoxy-beta-D-glucopyranose C8 H15 N O6 OVRNDRQMDRJTHS-FMDGEEDCSA-N |  | ||
| SO4 Query on SO4 | H [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |  | ||
| GOL Query on GOL | E [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| CL Query on CL | F [auth A], G [auth A] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 2.20 Å
- R-Value Free: 0.237
- R-Value Work: 0.209
- R-Value Observed: 0.210
- Space Group: I 21 3
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 173.759 | α = 90 |
| b = 173.759 | β = 90 |
| c = 173.759 | γ = 90 |
| Software Name | Purpose |
|---|---|
| ADSC | data collection |
| PHASES | phasing |
| REFMAC | refinement |
| HKL-2000 | data reduction |
| HKL-2000 | data scaling |
Entry History
Revision History (Full details and data files)
- Version 1.0: 2014-10-22
Type: Initial release - Version 1.1: 2017-06-28
Changes: Source and taxonomy - Version 1.2: 2020-07-29
Type: Remediation
Reason: Carbohydrate remediation
Changes: Data collection, Database references, Derived calculations, Structure summary - Version 1.3: 2023-11-08
Changes: Data collection, Database references, Refinement description, Structure summary
