5FFQ

ChuY: An Anaerobillin Reductase from Escherichia coli O157:H7

> Summary

Summary for 5FFQ

DescriptorShuY-like protein
Functional Keywordsnadph oxidoreductase, unknown function
Biological sourceEscherichia coli O157:H7
Total number of polymer chains2
Total molecular weight43951.79
Authors
LaMattina, J.L.,Reedy, A.N.,Uy, K.G.,Lanzilotta, W.N. (deposition date: 2015-12-18, release date: 2017-01-11)
Primary citation
Lanzilotta, W.N.
A radical new paradigm for heme degradation
To Be Published,
Experimental method
X-RAY DIFFRACTION (2 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.217200.3%1.5%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

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

> Structural details

Entity

Chain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
A, BShuY-like proteinpolymer20721835.92
UniProt (Q8X5N4)
Pfam (PF13460)
Escherichia coli O157:H7Uncharacterized protein
PHOSPHATE IONnon-polymer95.02
1,4-BUTANEDIOLnon-polymer90.11
waterwater18.0342

Sequence viewer

Contents of the asymmetric unit

PolymersNumber of chains2
Total molecular weight43671.7
Non-Polymers*Number of molecules3
Total molecular weight280.1
All*Total molecular weight43951.8
*Water molecules are not included.

> Experimental details

Refinement Statistics

Experimental method:X-RAY DIFFRACTION (2 Å)

Cell axes50.48663.20166.535
Cell angles90.00106.6790.00
SpacegroupP 1 21 1
Resolution limits38.40 - 2.00
the highest resolution shell value2.080 - 2.000
R-factor0.1806
R-work0.17840
the highest resolution shell value0.209
R-free0.22040
the highest resolution shell value0.259
RMSD bond length0.008
RMSD bond angle0.999

Data Collection Statistics

Resolution limits38.40 - 2.00
the highest resolution shell value -
Number of reflections27184
Completeness99.7
Redundancy2

Crystallization Conditions

crystal IDmethodpHpH rangetemperatureunit
1VAPOR DIFFUSION, HANGING DROP5.6291

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
AC17binding site for residue PO4 A 301
ChainResidue
AGLY13
AVAL14
ALEU153
AARG176
AHOH414
AHOH415
AHOH465

AC26binding site for residue PO4 B 301
ChainResidue
BGLY13
BVAL14
BLEU153
BARG176
BHOH413
BHOH466

AC38binding site for residue BU1 B 302
ChainResidue
AGLY110
ATHR132
BSER136
BGLN139
BHOH404
BHOH406
BHOH484
BHOH537

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

site_idNumber of ResiduesDetails
BU1_5ffq_B_30291,4-BUTANEDIOL binding site
ChainResidueligand
AGLY110-ASP111BU1: 1,4-BUTANEDIOL
ATRP113-PRO114BU1: 1,4-BUTANEDIOL
ATHR132BU1: 1,4-BUTANEDIOL
ASER136BU1: 1,4-BUTANEDIOL
BSER136BU1: 1,4-BUTANEDIOL
BGLN139-THR140BU1: 1,4-BUTANEDIOL

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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

> Sequence Neighbor

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