Download MendeleyComplex structure of BCL-XL and mutated BIM BH3 domain
Ha, N.C., Kim, J.S.To be published.
4YK9
Complex structure of BCL-XL and mutated BIM BH3 domain
- PDB DOI: https://doi.org/10.2210/pdb4YK9/pdb
- Classification: APOPTOSIS
- Organism(s): Mus musculus, synthetic construct
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2015-03-04 Released: 2016-04-13
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.70 Å
- R-Value Free: 0.228
- R-Value Work: 0.192
- R-Value Observed: 0.194
wwPDB Validation 3D Report Full Report
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 |
| Bcl-2-like protein 1 | A, C [auth F] | 195 | Mus musculus | Mutation(s): 0 Gene Names: Bcl2l1, Bcl2l, Bclx |  |
UniProt | |||||
Find proteins for Q64373 (Mus musculus) Explore Q64373 Go to UniProtKB: Q64373 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q64373 | ||||
Sequence AnnotationsExpand | |||||
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Find similar proteins by: Sequence | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| BH3BIM | B, D [auth G] | 21 | synthetic construct | Mutation(s): 0 |  |
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
Sequence AnnotationsExpand | |||||
| |||||
Small Molecules
| Ligands 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
| ACT Query on ACT | E [auth A], H [auth A], I [auth F] | ACETATE ION C2 H3 O2 QTBSBXVTEAMEQO-UHFFFAOYSA-M |  | ||
| CL Query on CL | F [auth A], G [auth A], J [auth F] | CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M |  | ||
| Modified Residues 2 Unique | |||||
|---|---|---|---|---|---|
| ID | Chains | Type | Formula | 2D Diagram | Parent |
| AAR Query on AAR | B, D [auth G] | L-PEPTIDE LINKING | C6 H16 N5 O |  | ARG |
| SEP Query on SEP | B, D [auth G] | L-PEPTIDE LINKING | C3 H8 N O6 P |  | SER |
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.70 Å
- R-Value Free: 0.228
- R-Value Work: 0.192
- R-Value Observed: 0.194
- Space Group: P 3
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 81.738 | α = 90 |
| b = 81.738 | β = 90 |
| c = 42.568 | γ = 120 |
| Software Name | Purpose |
|---|---|
| PHENIX | refinement |
| HKL-2000 | data processing |
| Coot | model building |
| MOLREP | phasing |
Entry History
Revision History (Full details and data files)
- Version 1.0: 2016-04-13
Type: Initial release
