Download MendeleyCrystal structure of human beta-hydroxyisobutyryl-CoA hydrolase in complex with quercetin.
Pilka, E.S., Phillips, C., King, O.N.F., Guo, K., von Delft, F., Pike, A.C.W., Arrowsmith, C.H., Weigelt, J., Edwards, A.M., Oppermann, U.To be published.
3BPT
Crystal structure of human beta-hydroxyisobutyryl-CoA hydrolase in complex with quercetin
- PDB DOI: https://doi.org/10.2210/pdb3BPT/pdb
- Classification: HYDROLASE
- Organism(s): Homo sapiens
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2007-12-19 Released: 2008-01-08
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.50 Å
- R-Value Free: 0.197
- R-Value Work: 0.147
- R-Value Observed: 0.149
This is version 1.3 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 |
| 3-hydroxyisobutyryl-CoA hydrolase | 363 | Homo sapiens | Mutation(s): 0 Gene Names: HIBCH EC: 3.1.2.4 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q6NVY1 (Homo sapiens) Explore Q6NVY1 Go to UniProtKB: Q6NVY1 | |||||
PHAROS: Q6NVY1 GTEx: ENSG00000198130 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q6NVY1 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| QUE Query on QUE | B [auth A] | 3,5,7,3',4'-PENTAHYDROXYFLAVONE C15 H10 O7 REFJWTPEDVJJIY-UHFFFAOYSA-N |  | ||
| HIU Query on HIU | C [auth A] | (2R)-3-HYDROXY-2-METHYLPROPANOIC ACID C4 H8 O3 DBXBTMSZEOQQDU-GSVOUGTGSA-N |  | ||
| Modified Residues 1 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| MSE Query on MSE | A | L-PEPTIDE LINKING | C5 H11 N O2 Se |  | MET |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.50 Å
- R-Value Free: 0.197
- R-Value Work: 0.147
- R-Value Observed: 0.149
- Space Group: P 1 21 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 44.096 | α = 90 |
| b = 76.642 | β = 108.24 |
| c = 55.789 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| MOSFLM | data reduction |
| SCALEPACK | data scaling |
| SHELXD | phasing |
Entry History
Deposition Data
- Released Date: 2008-01-08 Deposition Author(s): Pilka, E.S., Phillips, C., King, O.N.F., Guo, K., von Delft, F., Pike, A.C.W., Arrowsmith, C.H., Weigelt, J., Edwards, A.M., Oppermann, U., Structural Genomics Consortium (SGC)
Revision History (Full details and data files)
- Version 1.0: 2008-01-08
Type: Initial release - Version 1.1: 2011-07-13
Changes: Advisory, Version format compliance - Version 1.2: 2017-10-25
Changes: Refinement description - Version 1.3: 2024-10-09
Changes: Data collection, Database references, Derived calculations, Structure summary
