5LNN

Crystal structure of D1050A mutant of the receiver domain of the histidine kinase CKI1 from Arabidopsis thaliana

> Summary

Summary for 5LNN

Related3MMN 3MM4 5F0T
DescriptorHistidine kinase CKI1 (2 entities in total)
Functional Keywordsreceiver domain, mutant, histidine kinase cki1, (alpha/beta)5 fold, transferase
Biological sourceArabidopsis thaliana (Mouse-ear cress)
Cellular locationCell membrane ; Multi-pass membrane protein  O22267
Total number of polymer chains1
Total molecular weight23181.87
Authors
Primary citation
Otrusinova, O.,Demo, G.,Padrta, P.,Jasenakova, Z.,Pekarova, B.,Gelova, Z.,Szmitkowska, A.,Kaderavek, P.,Jansen, S.,Zachrdla, M.,Klumpler, T.,Marek, J.,Hritz, J.,Janda, L.,Iwai, H.,Wimmerova, M.,Hejatko, J.,Zidek, L.
Conformational dynamics as a key factor of signaling mediated by the receiver domain of sensor histidine kinase from Arabidopsis thaliana.
J. Biol. Chem., 2017
PubMed: 28860196 (PDB entries with the same primary citation)
DOI: 10.1074/jbc.M117.790212
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.6 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.23160.7%02.7%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

Molmil generated image of 5lnn
no rotation
Molmil generated image of 5lnn
rotated about x axis by 90°
Molmil generated image of 5lnn
rotated about y axis by 90°

> Structural details

Entity

Chain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
AHistidine kinase CKI1polymer20623181.91
UniProt (O22267)
Pfam (PF00072)
Arabidopsis thaliana (Mouse-ear cress)Protein CYTOKININ-INDEPENDENT 1
waterwater18.0137

Sequence viewer

Contents of the asymmetric unit

PolymersNumber of chains1
Total molecular weight23181.9
Non-Polymers*Number of molecules0
Total molecular weight0.0
All*Total molecular weight23181.9
*Water molecules are not included.

> Experimental details

Refinement Statistics

Experimental method:X-RAY DIFFRACTION (1.6 Å)

Cell axes53.176101.00579.464
Cell angles90.0090.0090.00
SpacegroupC 2 2 21
Resolution limits42.51 - 1.60
the highest resolution shell value1.642 - 1.600
R-factor0.19418
R-work0.19240
the highest resolution shell value0.225
R-free0.22806
the highest resolution shell value0.241
RMSD bond length0.026
RMSD bond angle2.377

Data Collection Statistics

Resolution limits47.05 - 1.60
the highest resolution shell value -
Number of reflections28315
Rmerge_l_obs0.023
the highest resolution shell value0.175
Completeness98.9
Redundancy6.4
the highest resolution shell value3.6

Crystallization Conditions

crystal IDmethodpHpH rangetemperatureunit
1VAPOR DIFFUSION, HANGING DROP5.05290.15

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
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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

site_idNumber of ResiduesDetails
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Functional Information from PROSITE/UniProt

site_idNumber of ResiduesDetails
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Functional Information from SwissProt/UniProt

site_idNumber of ResiduesDetails
SWS_FT_FI142Helical. {ECO:0000255}.
ChainResidueDetails
ANA*
ANA*

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Catalytic Information from CSA

site_idNumber of ResiduesDetails

> Sequence Neighbor

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