1YGW

NMR STRUCTURE OF RIBONUCLEASE T1, 34 STRUCTURES

> Summary

Summary for 1YGW

DescriptorRIBONUCLEASE T1
Functional Keywordshydrolase, ribonuclease, endonuclease, ribonuclease t1 precursor, endoribonuclease
Biological sourceAspergillus oryzae
Total number of polymer chains1
Total molecular weight11094.78
Authors
Pfeiffer, S.,Karimi-Nejad, Y.,Ruterjans, H. (deposition date: 1996-09-28, release date: 1997-10-08, modification date: 2009-02-24)
Primary citation
Pfeiffer, S.,Karimi-Nejad, Y.,Ruterjans, H.
Limits of NMR structure determination using variable target function calculations: ribonuclease T1, a case study.
J.Mol.Biol., 266:400-423, 1997
PubMed: 9047372
DOI: 10.1006/jmbi.1996.0784
MImport into Mendeley
Experimental method
SOLUTION NMR
NMR Information
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Structure validation

ClashscoreRamachandran outliersSidechain outliers18512.9%27.9%MetricValuePercentile RanksWorseBetterPercentile relative to all structuresPercentile relative to all NMR structures

More Asymmetric unit images

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

> Structural details

Entity

Chain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
ARIBONUCLEASE T1polymer10411094.81
UniProt (P00651)
Pfam (PF00545)
Aspergillus oryzae@PDBjGUANYLORIBONUCLEASE, RNASE T1

Sequence viewer

Contents of the asymmetric unit

PolymersNumber of chains1
Total molecular weight11094.8
Non-Polymers*Number of molecules0
Total molecular weight0.0
All*Total molecular weight11094.8
*Water molecules are not included.

> Experimental details

Spectrometer

Experimental method:SOLUTION NMR

Spectrometer IDSpectrometer makerSpectrometer modelSpectrometer typeSpectrometer field strength
1BRUKERAMX600
2BRUKERDMX600

Experiment

experiment idconditions idsolution idExperiment type

NMR Sample

conditions idNMR sample pHNMR sample pressureNMR sample temperature
15.5313

Conformers

Conformers Calculated Total Number50
Conformers Submitted Total Number34

> Functional details

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Functional Information from GO Data

ChainGOidnamespacecontents
A0030428cellular_componentcell septum
A0001411cellular_componenthyphal tip
A0004521molecular_functionendoribonuclease activity
A0046589molecular_functionribonuclease T1 activity
A0003723molecular_functionRNA binding
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Functional Information from PDB Data

site_idNumber of ResiduesDetails
REC6GUANINE RECOGNITION SITE.
ChainResidue
ATYR42
AASN43
AASN44
ATYR45
AGLU46
AASN98

CAT5CATALYTIC SITE.
ChainResidue
ATYR38
AHIS40
AGLU58
AARG77
AHIS92

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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_FI11Proton donor.
ChainResidueDetails
AHIS92

SWS_FT_FI21Proton acceptor.
ChainResidueDetails
AGLU58

SWS_FT_FI31
ChainResidueDetails
AHIS40

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Catalytic Information from CSA

site_idNumber of ResiduesDetails
CSA13Annotated By Reference To The Literature 1b2m
ChainResidueDetails
AGLU58
AHIS40
AHIS92

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Catalytic Information from CATRES

site_idNumber of ResiduesDetails

> Sequence Neighbor

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