2JET

CRYSTAL STRUCTURE OF A TRYPSIN-LIKE MUTANT (S189D, A226G) CHYMOTRYPSIN.

> Summary

Summary for 2JET

Related1KDQ
DescriptorCHYMOTRYPSINOGEN B CHAIN A (E.C.3.4.21.1), CHYMOTRYPSINOGEN B CHAIN B (E.C.3.4.21.1), CHYMOTRYPSINOGEN B CHAIN C (E.C.3.4.21.1)
Functional Keywordssubstrate specificity, zymogen, protease, hydrolase, digestion, serine protease, protein engineering
Biological sourceRATTUS NORVEGICUS (RAT)
Cellular locationSecreted, extracellular space P07338 P07338 P07338
Total number of polymer chains3
Total molecular weight25679.25
Authors
Jelinek, B.,Katona, G.,Fodor, K.,Venekei, I.,Graf, L. (deposition date: 2007-01-22, release date: 2007-09-18, modification date: 2011-07-13)
Primary citation
Jelinek, B.,Katona, G.,Fodor, K.,Venekei, I.,Graf, L.
The Crystal Structure of a Trypsin-Like Mutant Chymotrypsin: The Role of Position 226 in the Activity and Specificity of S189D Chymotrypsin.
Protein J., 27:79-, 2008
PubMed: 17805946
DOI: 10.1007/S10930-007-9110-3
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.2 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.35151.4%1.1%52.2%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

Molmil generated image of 2jet
no rotation
Molmil generated image of 2jet
rotated about x axis by 90°
Molmil generated image of 2jet
rotated about y axis by 90°

> Structural details

Sequence viewer

Contents of the asymmetric unit

PolymersNumber of chains3
Total molecular weight25679.2
Non-Polymers*Number of molecules0
Total molecular weight0.0
All*Total molecular weight25679.2
*Water molecules are not included.

> Experimental details

Refinement Statistics

Experimental method:X-RAY DIFFRACTION (2.2 Å)

Cell axes34.69064.35144.224
Cell angles90.00102.0990.00
SpacegroupP 1 21 1
Resolution limits43.23 - 2.20
the highest resolution shell value2.260 - 2.200
R-factor0.279
R-work0.27600
the highest resolution shell value0.316
R-free0.33400
the highest resolution shell value0.360
RMSD bond length0.005
RMSD bond angle0.824

Data Collection Statistics

Resolution limits64.42 - 2.20
the highest resolution shell value -
Number of reflections9753
Rmerge_l_obs0.090
the highest resolution shell value0.440
Completeness98.5
Redundancy3.1
the highest resolution shell value2.8
I/sigma(I)2

Crystallization Conditions

crystal IDmethodpHpH rangetemperatureunit
17

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
A0005737cellular_componentcytoplasm
A0005615cellular_componentextracellular space
A0005764cellular_componentlysosome
A0004252molecular_functionserine-type endopeptidase activity
A0007586biological_processdigestion
A0043065biological_processpositive regulation of apoptotic process
A0030163biological_processprotein catabolic process
A0034097biological_processresponse to cytokine
A0032094biological_processresponse to food
A0007584biological_processresponse to nutrient
A0043434biological_processresponse to peptide hormone
A0009636biological_processresponse to toxic substance
B0005737cellular_componentcytoplasm
B0005615cellular_componentextracellular space
B0005764cellular_componentlysosome
B0004252molecular_functionserine-type endopeptidase activity
B0007586biological_processdigestion
B0043065biological_processpositive regulation of apoptotic process
B0030163biological_processprotein catabolic process
B0034097biological_processresponse to cytokine
B0032094biological_processresponse to food
B0007584biological_processresponse to nutrient
B0043434biological_processresponse to peptide hormone
B0009636biological_processresponse to toxic substance
C0005737cellular_componentcytoplasm
C0005615cellular_componentextracellular space
C0005764cellular_componentlysosome
C0004252molecular_functionserine-type endopeptidase activity
C0007586biological_processdigestion
C0043065biological_processpositive regulation of apoptotic process
C0030163biological_processprotein catabolic process
C0034097biological_processresponse to cytokine
C0032094biological_processresponse to food
C0007584biological_processresponse to nutrient
C0043434biological_processresponse to peptide hormone
C0009636biological_processresponse to toxic substance
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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
PS001351Serine proteases, trypsin family, serine active site. [DNSTAGC]-[GSTAPIMVQH]-x(2)-G-[DE]-S-G-[GS]-[SAPHV]-[LIVMFYWH]
ChainResidueDetails
CNA*

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Functional Information from SwissProt/UniProt

site_idNumber of ResiduesDetails
SWS_FT_FI13Charge relay system (By similarity).
ChainResidueDetails
ANA*
ANA*
ANA*

SWS_FT_FI23Charge relay system (By similarity).
ChainResidueDetails
BHIS39
BASP84
BNA*

SWS_FT_FI33Charge relay system (By similarity).
ChainResidueDetails
CNA*
CNA*
CSER49

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Catalytic Information from CSA

site_idNumber of ResiduesDetails
CSA12Annotated By Reference To The Literature 1hja
ChainResidueDetails
CSER195
CGLY193

CSA24Annotated By Reference To The Literature 1hja
ChainResidueDetails
CSER195
CGLY196
BASP102
BHIS57

> Sequence Neighbor

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