2YED

HSP90 inhibitors and drugs from fragment and virtual screening

PDB DOI: https://doi.org/10.2210/pdb2YED/pdb

Classification: CHAPERONE
Organism(s): Homo sapiens
Expression System: Escherichia coli BL21(DE3)
Mutation(s): No

Deposited: 2011-03-25 Released: 2011-06-15
Deposition Author(s): Roughley, S.D., Hubbard, R.E., Baker, L.M.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.10 Å
R-Value Free: 0.258
R-Value Work: 0.206
R-Value Observed: 0.208

Starting Model: experimental
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wwPDB Validation 3D Report Full Report

This is version 1.3 of the entry. See complete history.

Literature

How Well Can Fragments Explore Accessed Chemical Space? a Case Study from Heat Shock Protein 90.

Roughley, S.D., Hubbard, R.E.

(2011) J Med Chem 54: 3989

PubMed: 21561141 Search on PubMed
DOI: https://doi.org/10.1021/jm200350g
Primary Citation of Related Structures:
2YE2, 2YE3, 2YE4, 2YE5, 2YE6, 2YE7, 2YE8, 2YE9, 2YEA, 2YEB, 2YEC, 2YED, 2YEE, 2YEF, 2YEG, 2YEH, 2YEI, 2YEJ

Organizational Affiliation

Vernalis (R&D) Ltd., Granta Park, Abington, Cambridge, CB21 6GB, UK.

Macromolecule Content

Total Structure Weight: 28.69 kDa
Atom Count: 1,862
Modelled Residue Count: 209
Deposited Residue Count: 252
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 PROTEIN HSP 90-ALPHA	A	252	Homo sapiens	Mutation(s): 0 EC: 3.6.4.10
UniProt & NIH Common Fund Data Resources
Find proteins for P07900 (Homo sapiens) Explore P07900 Go to UniProtKB: P07900
PHAROS: P07900 GTEx: ENSG00000080824
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P07900
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 2 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
ADE Query on ADE Download Ideal Coordinates CCD File SDF format, chain C [auth A] MOL2 format, chain C [auth A] mmCIF format, chain C [auth A]	C [auth A]	ADENINE C₅ H₅ N₅ GFFGJBXGBJISGV-UHFFFAOYSA-N		Interactions Focus chain C [auth A] Interactions & Density Focus chain C [auth A]
CL Query on CL Download Ideal Coordinates CCD File SDF format, chain B [auth A] MOL2 format, chain B [auth A] mmCIF format, chain B [auth A]	B [auth A]	CHLORIDE ION Cl VEXZGXHMUGYJMC-UHFFFAOYSA-M		Interactions Focus chain B [auth A] Interactions & Density Focus chain B [auth A]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.10 Å
R-Value Free: 0.258
R-Value Work: 0.206
R-Value Observed: 0.208
Space Group: I 2 2 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 65.326	α = 90
b = 89.194	β = 90
c = 99.888	γ = 90

Software Package:

Software Name	Purpose
REFMAC	refinement
d*TREK	data reduction
d*TREK	data scaling
AMoRE	phasing

Structure Validation

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Entry History

Deposition Data

Released Date: 2011-06-15

Deposition Author(s):

Roughley, S.D.

Hubbard, R.E.

Baker, L.M.

Revision History (Full details and data files)

Version 1.0: 2011-06-15
Type: Initial release
Version 1.1: 2011-06-23
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2023-12-20
Changes: Data collection, Database references, Derived calculations, Other, Refinement description

Prepare Data

Validate Data

Deposit Data

Help and Resources

2YED

HSP90 inhibitors and drugs from fragment and virtual screening

How Well Can Fragments Explore Accessed Chemical Space? a Case Study from Heat Shock Protein 90.

Entity ID: 1

UniProt & NIH Common Fund Data Resources

Entity Groups

Sequence Annotations

Expand

Experimental Data

Structure Validation

Deposition Data

Revision History (Full details and data files)