Download MendeleyCrystal Structure of human BFL-1 in complex with tBid BH3 peptide
Guan, R., Xiao, R., Mao, L., Gelinas, C., Montelione, G.T.To be published.
4ZEQ
Crystal Structure of human BFL-1 in complex with tBid BH3 peptide, Northeast Structural Genomics Consortium Target HX9247
- PDB DOI: https://doi.org/10.2210/pdb4ZEQ/pdb
- Classification: APOPTOSIS
- Organism(s): Homo sapiens
- Expression System: Escherichia coli
- Mutation(s): No
- Deposited: 2015-04-20 Released: 2015-05-06
- Funding Organization(s): National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
Experimental Data Snapshot
- Method: X-RAY DIFFRACTION
- Resolution: 1.80 Å
- R-Value Free: 0.239
- R-Value Work: 0.196
- R-Value Observed: 0.198
wwPDB Validation 3D Report Full Report
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 |
| Bcl-2-related protein A1 | 161 | Homo sapiens | Mutation(s): 0 Gene Names: BCL2A1, BCL2L5, BFL1, GRS, HBPA1 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for Q16548 (Homo sapiens) Explore Q16548 Go to UniProtKB: Q16548 | |||||
PHAROS: Q16548 GTEx: ENSG00000140379 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | Q16548 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Find similar proteins by:
(by identity cutoff) | 3D Structure
Entity ID: 2 | |||||
|---|---|---|---|---|---|
| Molecule | Chains | Sequence Length | Organism | Details | Image |
| BH3-interacting domain death agonist | 26 | Homo sapiens | Mutation(s): 0 |  | |
UniProt & NIH Common Fund Data Resources | |||||
Find proteins for P55957 (Homo sapiens) Explore P55957 Go to UniProtKB: P55957 | |||||
PHAROS: P55957 GTEx: ENSG00000015475 | |||||
Entity Groups | |||||
| Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
| UniProt Group | P55957 | ||||
Sequence AnnotationsExpand | |||||
| |||||
Experimental Data & Validation
Experimental Data
- Method: X-RAY DIFFRACTION
- Resolution: 1.80 Å
- R-Value Free: 0.239
- R-Value Work: 0.196
- R-Value Observed: 0.198
- Space Group: P 1 21 1
Unit Cell:
| Length ( Å ) | Angle ( ˚ ) |
|---|---|
| a = 43.339 | α = 90 |
| b = 43.469 | β = 114.21 |
| c = 46.263 | γ = 90 |
| Software Name | Purpose |
|---|---|
| REFMAC | refinement |
| d*TREK | data reduction |
| d*TREK | data scaling |
| PHASER | phasing |
Entry History & Funding Information
Deposition Data
- Released Date: 2015-05-06 Deposition Author(s): Guan, R., Xiao, R., Mao, L., Montelione, G.T., Northeast Structural Genomics Consortium (NESG)
| Funding Organization | Location | Grant Number |
|---|---|---|
| National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) | United States | -- |
Revision History (Full details and data files)
- Version 1.0: 2015-05-06
Type: Initial release - Version 1.1: 2016-07-20
Changes: Data collection - Version 1.2: 2019-11-27
Changes: Author supporting evidence, Derived calculations - Version 1.3: 2023-09-27
Changes: Data collection, Database references, Refinement description
