5HDK

Crystal structure of heat shock factor 2-DBD

PDB DOI: https://doi.org/10.2210/pdb5HDK/pdb

Classification: TRANSCRIPTION
Organism(s): Homo sapiens
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2016-01-05 Released: 2017-01-11
Deposition Author(s): Feng, H., Liu, W., Wang, D.C.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.32 Å
R-Value Free: 0.174
R-Value Work: 0.153
R-Value Observed: 0.153

wwPDB Validation 3D Report Full Report

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

Literature

HSF1-DBD crystal structure

Feng, H., Liu, W., Wang, D.C.

To be published.

Macromolecule Content

Total Structure Weight: 54.17 kDa
Atom Count: 4,058
Modelled Residue Count: 400
Deposited Residue Count: 448
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Heat shock factor protein 2	A, B, C, D	112	Homo sapiens	Mutation(s): 0 Gene Names: HSF2, HSTF2
UniProt & NIH Common Fund Data Resources
Find proteins for Q03933 (Homo sapiens) Explore Q03933 Go to UniProtKB: Q03933
PHAROS: Q03933 GTEx: ENSG00000025156
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	Q03933
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 3 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
K Query on K Download Ideal Coordinates CCD File SDF format, chain E [auth A] SDF format, chain I [auth B] SDF format, chain N [auth C] SDF format, chain P [auth D] SDF format, chain Q [auth D] SDF format, chain R [auth D] MOL2 format, chain E [auth A] MOL2 format, chain I [auth B] MOL2 format, chain N [auth C] MOL2 format, chain P [auth D] MOL2 format, chain Q [auth D] MOL2 format, chain R [auth D]	E [auth A] I [auth B] N [auth C] P [auth D] Q [auth D] E [auth A], I [auth B], N [auth C], P [auth D], Q [auth D], R [auth D]	POTASSIUM ION K NPYPAHLBTDXSSS-UHFFFAOYSA-N		Interactions Focus chain E [auth A] Focus chain I [auth B] Focus chain N [auth C] Focus chain P [auth D] Focus chain Q [auth D] Focus chain R [auth D] Interactions & Density Focus chain E [auth A] Focus chain I [auth B] Focus chain N [auth C] Focus chain P [auth D] Focus chain Q [auth D] Focus chain R [auth D]
CL Query on CL Download Ideal Coordinates CCD File SDF format, chain J [auth B] SDF format, chain S [auth D] SDF format, chain T [auth D] MOL2 format, chain J [auth B] MOL2 format, chain S [auth D] MOL2 format, chain T [auth D]	J [auth B], S [auth D], T [auth D]	CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M		Interactions Focus chain J [auth B] Focus chain S [auth D] Focus chain T [auth D] Interactions & Density Focus chain J [auth B] Focus chain S [auth D] Focus chain T [auth D]
NA Query on NA Download Ideal Coordinates CCD File SDF format, chain F [auth A] SDF format, chain G [auth A] SDF format, chain H [auth A] SDF format, chain K [auth B] SDF format, chain L [auth B] SDF format, chain M [auth B] SDF format, chain O [auth C] SDF format, chain U [auth D] SDF format, chain V [auth D] MOL2 format, chain F [auth A] MOL2 format, chain G [auth A] MOL2 format, chain H [auth A] MOL2 format, chain K [auth B] MOL2 format, chain L [auth B] MOL2 format, chain M [auth B] MOL2 format, chain O [auth C] MOL2 format, chain U [auth D] MOL2 format, chain V [auth D]	F [auth A] G [auth A] H [auth A] K [auth B] L [auth B] F [auth A], G [auth A], H [auth A], K [auth B], L [auth B], M [auth B], O [auth C], U [auth D], V [auth D]	SODIUM ION Na FKNQFGJONOIPTF-UHFFFAOYSA-N		Interactions Focus chain F [auth A] Focus chain G [auth A] Focus chain H [auth A] Focus chain K [auth B] Focus chain L [auth B] Focus chain M [auth B] Focus chain O [auth C] Focus chain U [auth D] Focus chain V [auth D] Interactions & Density Focus chain F [auth A] Focus chain G [auth A] Focus chain H [auth A] Focus chain K [auth B] Focus chain L [auth B] Focus chain M [auth B] Focus chain O [auth C] Focus chain U [auth D] Focus chain V [auth D]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.32 Å
R-Value Free: 0.174
R-Value Work: 0.153
R-Value Observed: 0.153
Space Group: P 2₁ 2₁ 2₁

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 65.66	α = 90
b = 67.26	β = 90
c = 93.25	γ = 90

Software Package:

Software Name	Purpose
PHENIX	refinement
XSCALE	data reduction
XDS	data scaling
XDS	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2017-01-11

Deposition Author(s):

Feng, H.

Liu, W.

Wang, D.C.

Revision History (Full details and data files)

Version 1.0: 2017-01-11
Type: Initial release
Version 1.1: 2017-09-27
Changes: Data collection
Version 1.2: 2023-11-08
Changes: Data collection, Database references, Derived calculations, Refinement description