5B1Z

Crystal structure of Bcl-xL in complex with HBx-BH3 motif

PDB DOI: https://doi.org/10.2210/pdb5B1Z/pdb

Classification: APOPTOSIS
Organism(s): Homo sapiens, Hepatitis B virus
Expression System: Escherichia coli BL21(DE3), Peptide display vector fth1
Mutation(s): No

Deposited: 2015-12-22 Released: 2016-12-28
Deposition Author(s): Yuan, Y.A.
Funding Organization(s): Ministry of Science and Technology

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.15 Å
R-Value Free: 0.274
R-Value Work: 0.205
R-Value Observed: 0.209

wwPDB Validation 3D Report Full Report

This is version 1.2 of the entry. See complete history.

Literature

Crystal structure of Bcl-xL in complex with HBx-BH3 motif

Yuan, Y.A.

To be published.

Macromolecule Content

Total Structure Weight: 40.53 kDa
Atom Count: 2,765
Modelled Residue Count: 322
Deposited Residue Count: 352
Unique protein chains: 2

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, B	153	Homo sapiens	Mutation(s): 0 Gene Names: BCL2L1, BCL2L, BCLX
UniProt & NIH Common Fund Data Resources
Find proteins for Q07817 (Homo sapiens) Explore Q07817 Go to UniProtKB: Q07817
PHAROS: Q07817 GTEx: ENSG00000171552
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q07817
Sequence Annotations Expand
Reference Sequence

Find similar proteins by: Sequence | 3D Structure

Entity ID: 2
Molecule	Chains	Sequence Length	Organism	Details	Image
Peptide from Protein X	C, D	23	Hepatitis B virus	Mutation(s): 0
UniProt
Find proteins for I3XMW8 (Hepatitis B virus) Explore I3XMW8 Go to UniProtKB: I3XMW8
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	I3XMW8
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.15 Å
R-Value Free: 0.274
R-Value Work: 0.205
R-Value Observed: 0.209
Space Group: C 2 2 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 50.708	α = 90
b = 135.317	β = 90
c = 97.593	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
HKL-2000	data reduction
HKL-2000	data scaling
MOLREP	phasing

Structure Validation

View Full Validation Report

Entry History & Funding Information

Deposition Data

Released Date: 2016-12-28

Deposition Author(s):

Funding Organization	Location	Grant Number
Ministry of Science and Technology	China	--

Revision History (Full details and data files)

Version 1.0: 2016-12-28
Type: Initial release
Version 1.1: 2017-10-04
Changes: Data collection
Version 1.2: 2024-03-20
Changes: Data collection, Database references

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.