2W0G

HSP90 CO-CHAPERONE CDC37

> Summary

Summary for 2W0G

Related1US7
DescriptorHSP90 CO-CHAPERONE CDC37 (2 entities in total)
Functional Keywordschaperone, heat shock, atp-binding, stress response, nucleotide-binding, phosphoprotein, phosphorylation, chaperone co-chaperone regulation
Biological sourceHOMO SAPIENS (HUMAN)
Cellular locationCytoplasm  Q16543
Total number of polymer chains1
Total molecular weight15521.08
Authors
Sreeramulu, S.,Jonker, H.R.A.,Schwalbe, H.,Lancaster, C.R.D. (deposition date: 2008-08-15, release date: 2008-12-09, Last modification date: 2017-07-05)
Primary citation
Sreeramulu, S.,Jonker, H.R.A.,Richter, C.,Langer, T.,Lancaster, C.R.D.,Schwalbe, H.
The Human Cdc37.Hsp90 Complex Studied by Heteronuclear NMR Spectroscopy.
J.Biol.Chem., 284:3885-, 2009
PubMed: 19073599 (PDB entries with the same primary citation)
DOI: 10.1074/JBC.M806715200
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.88 Å)
NMR Information
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.246606.8%2.4%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

Molmil generated image of 2w0g
no rotation
Molmil generated image of 2w0g
rotated about x axis by 90°
Molmil generated image of 2w0g
rotated about y axis by 90°

> Structural details

Entity

Chain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
AHSP90 CO-CHAPERONE CDC37polymer12915521.11
UniProt (Q16543)
Pfam (PF08565)
HOMO SAPIENS (HUMAN)@PDBjHSP90 CHAPERONE PROTEIN KINASE-TARGETING SUBUNIT, P50CDC37
waterwater18.074

Sequence viewer

Contents of the asymmetric unit

PolymersNumber of chains1
Total molecular weight15521.1
Non-Polymers*Number of molecules0
Total molecular weight0.0
All*Total molecular weight15521.1
*Water molecules are not included.

> Experimental details

Refinement Statistics

Experimental method:X-RAY DIFFRACTION (1.88 Å)

Cell axes48.67048.670104.257
Cell angles90.0090.00120.00
SpacegroupP 61
Resolution limits42.14 - 1.88
the highest resolution shell value1.930 - 1.880
R-factor0.213
R-work0.21200
the highest resolution shell value0.291
R-free0.24600
the highest resolution shell value0.450
RMSD bond length0.018
RMSD bond angle1.544

Data Collection Statistics

Resolution limits42.14 - 1.88
the highest resolution shell value -
Number of reflections11278
Rmerge_l_obs0.060
the highest resolution shell value0.310
Completeness98.7
Redundancy32.7
the highest resolution shell value36.8
I/sigma(I)-3

Crystallization Conditions

crystal IDmethodpHpH rangetemperatureunit

Crystallization Reagents

IDcrystal IDsolution IDreagent nameconcentrationdetails
Crystallization Reagents in Literatures*
IDcrystal IDsolutionreagent nameconcentration (unit)details
Annotated Information is extracted from Literature Info*

> Functional details

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Functional Information from GO Data

ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0070062cellular_componentextracellular exosome
A1990565cellular_componentHSP90-CDC37 chaperone complex
A0051087molecular_functionchaperone binding
A0031072molecular_functionheat shock protein binding
A0051879molecular_functionHsp90 protein binding
A0019900molecular_functionkinase binding
A0019901molecular_functionprotein kinase binding
A0019887molecular_functionprotein kinase regulator activity
A0004713molecular_functionprotein tyrosine kinase activity
A0051082molecular_functionunfolded protein binding
A0038128biological_processERBB2 signaling pathway
A0098779biological_processpositive regulation of mitophagy in response to mitochondrial depolarization
A0010608biological_processposttranscriptional regulation of gene expression
A0006457biological_processprotein folding
A0050821biological_processprotein stabilization
A0006605biological_processprotein targeting
A0000079biological_processregulation of cyclin-dependent protein serine/threonine kinase activity
A0060334biological_processregulation of interferon-gamma-mediated signaling pathway
A0060338biological_processregulation of type I interferon-mediated signaling pathway
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Functional Information from PDB Data

site_idNumber of ResiduesDetails
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Functional Information from PDB atom coordinates for the "HETATM" binding sites

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Functional Information from PROSITE/UniProt

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Functional Information from SwissProt/UniProt

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Catalytic Information from CSA

site_idNumber of ResiduesDetails

> Sequence Neighbor

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