1RQW

Thaumatin Structure at 1.05 A Resolution

> Summary

Summary for 1RQW

Descriptorthaumatin I
Functional Keywordsthaumatin; x-ray structure, plant protein
Biological sourceThaumatococcus daniellii (miracle fruit)
Cellular locationCytoplasmic vesicle P02883
Total number of polymer chains1
Total molecular weight22393.31
Authors
Ma, Q.,Sheldrick, G.M. (deposition date: 2003-12-07, release date: 2003-12-23, modification date: 2012-04-25)
Primary citation
Ma, Q.,Sheldrick, G.M.
Thaumatin Structure at 1.05 A Resolution
To be Published,
Experimental method
X-RAY DIFFRACTION (1.05 Å)
?

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.137603.0%2.9%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

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

> Structural details

Entity

Chain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
Athaumatin Ipolymer20722243.21
UniProt (P02883)
Thaumatococcus daniellii (miracle fruit)
L(+)-TARTARIC ACIDnon-polymer150.11
waterwater18.0398

Sequence viewer

Contents of the asymmetric unit

PolymersNumber of chains1
Total molecular weight22243.2
Non-Polymers*Number of molecules1
Total molecular weight150.1
All*Total molecular weight22393.3
*Water molecules are not included.

> Experimental details

Refinement Statistics

Experimental method:X-RAY DIFFRACTION (1.05 Å)
Cell axes57.84757.847150.125
Cell angles90.0090.0090.00
SpacegroupP 41 21 2
Resolution limits10.00 - 1.05
the highest resolution shell value -
R-factor0.127
R-free0.15200
RMSD bond length0.008
RMSD bond angle0.026

Data Collection Statistics

Resolution limits160.00 - 1.05
the highest resolution shell value -
Number of reflections116807
Completeness97.7
Redundancy19.1
the highest resolution shell value9.25
I/sigma(I)-3

Crystallization Conditions

crystal IDmethodpHpH rangetemperatureunit
16.8298

Crystallization Reagents

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

> Functional details

?

Functional Information from GO Data

ChainGOidnamespacecontents
A0016023cellular_componentcytoplasmic, membrane-bounded vesicle
?

Functional Information from PDB Data

site_idNumber of ResiduesDetails
AC112BINDING SITE FOR RESIDUE TLA A 1001
ChainResidue
AARG29
AGLU35
ASER36
APHE152
ATYR157
AHOH
AHOH
AHOH
AHOH
AHOH
AHOH
AHOH

?

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

site_idNumber of ResiduesDetails
TLA_1rqw_A_10016L(+)-TARTARIC ACID binding site
ChainResidueligand
AARG29TLA: L(+)-TARTARIC ACID
ALEU31TLA: L(+)-TARTARIC ACID
AGLY34-TRP37TLA: L(+)-TARTARIC ACID

?

Functional Information from PROSITE/UniProt

site_idNumber of ResiduesDetails
PS005831pfkB family of carbohydrate kinases signature 1. [AG]-G-x(0,1)-[GAP]-x-N-{AGLS}-[STA]-x(2)-{A}-x-{G}-{GNKA}-[GS]-x(9)-G
ChainResidueDetails
ANA*

PS003161Thaumatin family signature. G-x-[GF]-x-C-x-T-[GA]-D-C-x(1,2)-[GQ]-x(2,3)-C
ChainResidueDetails
ANA*

?

Functional Information from SwissProt/UniProt

site_idNumber of ResiduesDetails
?

Catalytic Information from CSA

site_idNumber of ResiduesDetails
?

Catalytic Information from CATRES

site_idNumber of ResiduesDetails

> Sequence Neighbor

> Downloads

Copyright © 2013-2016 Protein Data Bank Japan