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- PDB-1ane: ANIONIC TRYPSIN WILD TYPE -

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Basic information

Entry
Database: PDB / ID: 1ane
TitleANIONIC TRYPSIN WILD TYPE
ComponentsANIONIC TRYPSIN
KeywordsSERINE PROTEASE / TRYPSIN / ANIONIC / HYDROLASE
Function / homology
Function and homology information


Antimicrobial peptides / Alpha-defensins / Activation of Matrix Metalloproteinases / Collagen degradation / Neutrophil degranulation / collagen catabolic process / trypsin / digestion / response to nutrient / serine-type endopeptidase activity ...Antimicrobial peptides / Alpha-defensins / Activation of Matrix Metalloproteinases / Collagen degradation / Neutrophil degranulation / collagen catabolic process / trypsin / digestion / response to nutrient / serine-type endopeptidase activity / calcium ion binding / proteolysis / extracellular space / extracellular region
Similarity search - Function
Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, histidine active site. / Serine proteases, trypsin domain profile. / Serine proteases, trypsin family, serine active site. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Trypsin-like serine proteases ...Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, histidine active site. / Serine proteases, trypsin domain profile. / Serine proteases, trypsin family, serine active site. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Trypsin-like serine proteases / Thrombin, subunit H / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
BENZAMIDINE / Anionic trypsin-2
Similarity search - Component
Biological speciesRattus rattus (black rat)
MethodX-RAY DIFFRACTION / Resolution: 2.2 Å
AuthorsFletterick, R.J. / Mcgrath, M.E.
CitationJournal: Biochemistry / Year: 1993
Title: Structure of an engineered, metal-actuated switch in trypsin.
Authors: McGrath, M.E. / Haymore, B.L. / Summers, N.L. / Craik, C.S. / Fletterick, R.J.
History
DepositionDec 21, 1994-
Revision 1.0Apr 1, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: ANIONIC TRYPSIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)23,9352
Polymers23,8151
Non-polymers1201
Water2,234124
1
A: ANIONIC TRYPSIN
hetero molecules

A: ANIONIC TRYPSIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)47,8704
Polymers47,6302
Non-polymers2402
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation3_556-x,y,-z+11
Unit cell
Length a, b, c (Å)124.380, 124.380, 124.380
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number197
Space group name H-MI23

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Components

#1: Protein ANIONIC TRYPSIN


Mass: 23814.838 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus rattus (black rat) / Production host: Escherichia coli (E. coli) / References: UniProt: P00763, trypsin
#2: Chemical ChemComp-BEN / BENZAMIDINE / Benzamidine


Mass: 120.152 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C7H8N2
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 124 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.34 Å3/Da / Density % sol: 63 %
Crystal growpH: 8 / Details: pH 8.0

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Data collection

DiffractionMean temperature: 273 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RUH2R / Wavelength: 1.5418
DetectorType: SIEMENS / Detector: AREA DETECTOR / Date: 1992
RadiationMonochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1

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Processing

Software
NameClassification
BUDDHAdata collection
BUDDHAdata reduction
X-PLORrefinement
BUDDHAdata scaling
RefinementRfactor Rwork: 0.175 / Rfactor obs: 0.175 / Highest resolution: 2.2 Å
Refinement stepCycle: LAST / Highest resolution: 2.2 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1665 0 9 124 1798

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