1N11

D34 REGION OF HUMAN ANKYRIN-R AND LINKER

> Summary

Summary for 1N11

DescriptorAnkyrin
Functional Keywordsankyrin, clathrin, band 3, anion exchanger, structural protein
Biological sourceHomo sapiens (human)
Cellular locationIsoform Er1: Cytoplasm, cytoskeleton. Isoform Mu17: Membrane. Isoform Mu18: Sarcoplasmic reticulum (Probable). Isoform Mu19: Sarcoplasmic reticulum (Probable). Isoform Mu20: Sarcoplasmic reticulum (Probable) P16157
Total number of polymer chains1
Total molecular weight46859.45
Authors
Michaely, P.,Tomchick, D.R.,Machius, M.,Anderson, R.G.W. (deposition date: 2002-10-16, release date: 2002-12-11, modification date: 2009-02-24)
Primary citation
Michaely, P.,Tomchick, D.R.,Machius, M.,Anderson, R.G.W.
Crystal structure of a 12 ANK repeat stack from human ankyrinR
Embo J., 21:6387-6396, 2002
PubMed: 12456646
DOI: 10.1093/emboj/cdf651
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.7 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.304394.0%9.5%15.6%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

Molmil generated image of 1n11
no rotation
Molmil generated image of 1n11
rotated about x axis by 90°
Molmil generated image of 1n11
rotated about y axis by 90°

> Structural details

Entity

Chain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
AAnkyrinpolymer43746460.51
UniProt (P16157)
Pfam (PF00023)
Homo sapiens (human)@PDBj
BROMIDE IONnon-polymer79.91
CHLORIDE IONnon-polymer35.59

Sequence viewer

Contents of the asymmetric unit

PolymersNumber of chains1
Total molecular weight46460.5
Non-Polymers*Number of molecules10
Total molecular weight399.0
All*Total molecular weight46859.4
*Water molecules are not included.

> Experimental details

Refinement Statistics

Experimental method:X-RAY DIFFRACTION (2.7 Å)

Cell axes137.329137.329197.801
Cell angles90.0090.00120.00
SpacegroupP 63 2 2
Resolution limits30.00 - 2.70
the highest resolution shell value -
R-factor0.318
R-work0.31900
R-free0.30300
RMSD bond length0.010
RMSD bond angle1.620

Data Collection Statistics

Resolution limits50.00 - 2.50
the highest resolution shell value -
Number of reflections415031 (37994*)
Number of measurements415031*
Rmerge_l_obs0.082
the highest resolution shell value0.699
Completeness98.4
the highest resolution shell value93.*
I/sigma(I)0

Crystallization Conditions

crystal IDmethodpHpH rangetemperatureunit
1VAPOR DIFFUSION, HANGING DROP (Vapor diffusion*)7.5277 (4*)*

Crystallization Reagents

IDcrystal IDsolution IDreagent nameconcentrationdetails
Crystallization Reagents in Literatures*
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein25 (mg/ml)
21dropHEPES-Na20 (mM)pH7.5
31drop500 (mM)
41dropEDTA1 (mM)
51dropdithiothreitol1 (mM)
61reservoirHEPES100 (mM)pH7.5
71reservoir500 (mM)
81reservoirPEG4007-10 (%(v/v))
91reservoiracetonitrile5 (%(v/v))
Annotated Information is extracted from Literature Info*

> Functional details

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Functional Information from GO Data

ChainGOidnamespacecontents
A0030673cellular_componentaxolemma
A0016323cellular_componentbasolateral plasma membrane
A0005737cellular_componentcytoplasm
A0005856cellular_componentcytoskeleton
A0005829cellular_componentcytosol
A0031430cellular_componentM band
A0005634cellular_componentnucleus
A0005886cellular_componentplasma membrane
A0045211cellular_componentpostsynaptic membrane
A0042383cellular_componentsarcolemma
A0016529cellular_componentsarcoplasmic reticulum
A0014731cellular_componentspectrin-associated cytoskeleton
A0030018cellular_componentZ disc
A0051117molecular_functionATPase binding
A0008093molecular_functioncytoskeletal adaptor activity
A0019899molecular_functionenzyme binding
A0030507molecular_functionspectrin binding
A0005200molecular_functionstructural constituent of cytoskeleton
A0005198molecular_functionstructural molecule activity
A0007010biological_processcytoskeleton organization
A0006888biological_processER to Golgi vesicle-mediated transport
A0006887biological_processexocytosis
A0045199biological_processmaintenance of epithelial cell apical/basal polarity
A0010638biological_processpositive regulation of organelle organization
A0072661biological_processprotein targeting to plasma membrane
A0007165biological_processsignal transduction
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Functional Information from PDB Data

site_idNumber of ResiduesDetails
AC11BINDING SITE FOR RESIDUE BR A 1001
ChainResidue
ASER230

AC22BINDING SITE FOR RESIDUE CL A 1002
ChainResidue
AGLN354
AHIS356

AC31BINDING SITE FOR RESIDUE CL A 1003
ChainResidue
AHIS189

AC42BINDING SITE FOR RESIDUE CL A 1004
ChainResidue
AHIS189
AASN190

AC52BINDING SITE FOR RESIDUE CL A 1005
ChainResidue
ATHR307
ATHR308

AC63BINDING SITE FOR RESIDUE CL A 1006
ChainResidue
ALYS72
AVAL73
AASN74

AC73BINDING SITE FOR RESIDUE CL A 1007
ChainResidue
AHIS92
ATHR93
AASN94

AC81BINDING SITE FOR RESIDUE CL A 1008
ChainResidue
ACL

AC92BINDING SITE FOR RESIDUE CL A 1009
ChainResidue
AHIS188
ACL

BC14BINDING SITE FOR RESIDUE CL A 1010
ChainResidue
AALA286
AGLN287
AGLY322
AASN323

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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
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Catalytic Information from CSA

site_idNumber of ResiduesDetails
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Catalytic Information from CATRES

site_idNumber of ResiduesDetails

> Sequence Neighbor

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