Download MendeleyCrystal Structure of the Human CAMKK2B in complex with Crenolanib
Counago, R.M., de Souza, G.P., dos Reis, C.V., Drewry, D., Massirer, K.B., Arruda, P., Edwards, A.M., Elkins, J.M., Structural Genomics Consortium (SGC)To be published.
6BQP
Crystal Structure of the Human CAMKK2B in complex with Crenolanib
- PDB DOI: https://doi.org/10.2210/pdb6BQP/pdb
- Classification: TRANSFERASE
- Organism(s): Homo sapiens
- Expression System: Escherichia coli BL21(DE3)
- Mutation(s): No
- Deposited: 2017-11-28 Released: 2017-12-13
- Funding Organization(s): Sao Paulo Research Foundation (FAPESP)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.95 Å
- R-Value Free: 0.227
- R-Value Work: 0.189
- R-Value Observed: 0.191
Starting Model: experimental
View more details
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 |
| Calcium/calmodulin-dependent protein kinase kinase 2 | 291 | Homo sapiens | Mutation(s): 0 Gene Names: CAMKK2, CAMKKB, KIAA0787 EC: 2.7.11.17 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q96RR4 (Homo sapiens) Explore Q96RR4 Go to UniProtKB: Q96RR4 | |||||
PHAROS: Q96RR4 GTEx: ENSG00000110931 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q96RR4 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| 6T2 Query on 6T2 | B [auth A] | 1-(2-{5-[(3-Methyloxetan-3-yl)methoxy]-1H-benzimidazol-1-yl}quinolin-8-yl)piperidin-4-amine C26 H29 N5 O2 DYNHJHQFHQTFTP-UHFFFAOYSA-N |  | ||
| EDO Query on EDO | C [auth A] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N |  | ||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.95 Å
- R-Value Free: 0.227
- R-Value Work: 0.189
- R-Value Observed: 0.191
- Space Group: P 21 21 21
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 49.113 | α = 90 |
| b = 77.834 | β = 90 |
| c = 78.709 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| XDS | data reduction |
| Aimless | data scaling |
| PHASER | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2017-12-13 Deposition Author(s): Counago, R.M., de Souza, G.P., dos Reis, C.V., Ramos, P.Z., Drewry, D., Massirer, K.B., Arruda, P., Edwards, A.M., Elkins, J.M., Structural Genomics Consortium (SGC)
| Funding Organization | Location | Grant Number |
|---|---|---|
| Sao Paulo Research Foundation (FAPESP) | Brazil | 13/50724-5 |
Revision History (Full details and data files)
- Version 1.0: 2017-12-13
Type: Initial release - Version 1.1: 2019-04-17
Changes: Author supporting evidence, Data collection - Version 1.2: 2020-01-01
Changes: Author supporting evidence - Version 1.3: 2023-10-04
Changes: Data collection, Database references, Refinement description
