Download MendeleyCrystal structure of human secretory glutaminyl cyclase in complex with 1-benzyl-5-methyl-1H-imidazole
Li, G.-B., Deng, J.To be published.
8HY3
Crystal structure of human secretory glutaminyl cyclase in complex with 1-benzyl-5-methyl-1H-imidazole
- PDB DOI: https://doi.org/10.2210/pdb8HY3/pdb
- Classification: TRANSFERASE
- Organism(s): Homo sapiens
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2023-01-05 Released: 2024-05-08
- Funding Organization(s): National Natural Science Foundation of China (NSFC)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.95 Å
- R-Value Free: 0.258
- R-Value Work: 0.226
- R-Value Observed: 0.228
Starting Model: experimental
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This is version 1.0 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 |
| Glutaminyl-peptide cyclotransferase | 329 | Homo sapiens | Mutation(s): 0 Gene Names: QPCT EC: 2.3.2.5 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q16769 (Homo sapiens) Explore Q16769 Go to UniProtKB: Q16769 | |||||
PHAROS: Q16769 GTEx: ENSG00000115828 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q16769 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 4 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| 4Q8 (Subject of Investigation/LOI) Query on 4Q8 | C [auth A] | 5-methyl-1-(phenylmethyl)imidazole C11 H12 N2 BUKITYALZCIHTM-UHFFFAOYSA-N |  | ||
| GOL Query on GOL | E [auth A] | GLYCEROL C3 H8 O3 PEDCQBHIVMGVHV-UHFFFAOYSA-N |  | ||
| ZN Query on ZN | B [auth A] | ZINC ION Zn PTFCDOFLOPIGGS-UHFFFAOYSA-N |  | ||
| CO2 Query on CO2 | D [auth A] | CARBON DIOXIDE C O2 CURLTUGMZLYLDI-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.95 Å
- R-Value Free: 0.258
- R-Value Work: 0.226
- R-Value Observed: 0.228
- Space Group: F 41 3 2
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 273.952 | α = 90 |
| b = 273.952 | β = 90 |
| c = 273.952 | γ = 90 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| XDS | data scaling |
| XDS | data reduction |
| PHASER | phasing |
Entry History & Funding Information
Deposition Data
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Natural Science Foundation of China (NSFC) | China | 82122065;82073698;81874291 |
Revision History (Full details and data files)
- Version 1.0: 2024-05-08
Type: Initial release
