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- PDB-5cha: THE REFINEMENT AND THE STRUCTURE OF THE DIMER OF ALPHA-*CHYMOTRYP... -

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Basic information

Entry
Database: PDB / ID: 5cha
TitleTHE REFINEMENT AND THE STRUCTURE OF THE DIMER OF ALPHA-*CHYMOTRYPSIN AT 1.67-*ANGSTROMS RESOLUTION
Components(ALPHA-CHYMOTRYPSIN A) x 3
KeywordsHYDROLASE (SERINE PROTEINASE)
Function / homology
Function and homology information


chymotrypsin / serpin family protein binding / serine protease inhibitor complex / digestion / serine-type endopeptidase activity / proteolysis / 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 family, serine active site. / Serine proteases, trypsin domain profile. / 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 family, serine active site. / Serine proteases, trypsin domain profile. / 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
Biological speciesBos taurus (cattle)
MethodX-RAY DIFFRACTION / Resolution: 1.67 Å
AuthorsBlevins, R.A. / Tulinsky, A.
Citation
Journal: J.Biol.Chem. / Year: 1985
Title: The refinement and the structure of the dimer of alpha-chymotrypsin at 1.67-A resolution.
Authors: Blevins, R.A. / Tulinsky, A.
#1: Journal: Acta Crystallogr.,Sect.B / Year: 1986
Title: Least-Squares Refinement of Two Protein Molecules Per Asymmetric Unit with and without Non-Crystallographic Symmetry Restrained
Authors: Tulinsky, A. / Blevins, R.A.
#2: Journal: J.Biol.Chem. / Year: 1985
Title: Comparison of the Independent Solvent Structures of Dimeric Alpha-Chymotrypsin with Themselves and with Gamma-Chymotrypsin
Authors: Blevins, R.A. / Tulinsky, A.
#3: Journal: Acta Crystallogr.,Sect.B / Year: 1979
Title: The Structure of Alpha-Chymotrypsin. II. Fourier Phase Refinement and Extension of the Dimeric Structure at 1.8 Angstroms Resolution by Density Modification
Authors: Raghavan, N.V. / Tulinsky, A.
#4: Journal: Acta Crystallogr.,Sect.B / Year: 1973
Title: The Structure of Alpha-Chymotrypsin. I. The Refinement of the Heavy-Atom Isomorphous Derivatives at 2.8 Angstroms Resolution
Authors: Tulinsky, A. / Mani, N.V. / Morimoto, C.N. / Vandlen, R.L.
#5: Journal: Biochemistry / Year: 1973
Title: Variability in the Tertiary Structure of Alpha-Chymotrypsin at 2.8-Angstroms Resolution
Authors: Tulinsky, A. / Vandlen, R.L. / Morimoto, C.N. / Mani, N.V. / Wright, L.H.
#6: Journal: Biochemistry / Year: 1974
Title: Asymmetrical Changes in the Tertiary Structure of Alpha-Chymotrypsin with Change in Ph
Authors: Mavridis, A. / Tulinsky, A. / Liebman, M.N.
History
DepositionJan 22, 1985Processing site: BNL
SupersessionApr 1, 1985ID: 3CHA
Revision 1.0Apr 1, 1985Provider: repository / Type: Initial release
Revision 1.1Mar 3, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jun 5, 2024Group: Data collection / Database references / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site
Revision 1.4Oct 16, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: ALPHA-CHYMOTRYPSIN A
B: ALPHA-CHYMOTRYPSIN A
C: ALPHA-CHYMOTRYPSIN A
E: ALPHA-CHYMOTRYPSIN A
F: ALPHA-CHYMOTRYPSIN A
G: ALPHA-CHYMOTRYPSIN A


Theoretical massNumber of molelcules
Total (without water)50,5256
Polymers50,5256
Non-polymers00
Water4,450247
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15790 Å2
ΔGint-122 kcal/mol
Surface area18070 Å2
MethodPISA
Unit cell
Length a, b, c (Å)49.290, 67.480, 65.940
Angle α, β, γ (deg.)90.00, 102.02, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper: (Code: given
Matrix: (0.91387, -0.006906, 0.40595), (-0.006985, -0.999918, -0.012656), (0.406002, 0.010876, -0.913807)
Vector: -9.94, 40.6, 47.6)
Details5CHA THE TRANSFORMATION PROVIDED ON THE *MTRIX* RECORDS BELOW 5CHA YIELDS APPROXIMATE COORDINATES FOR CHAIN *A* WHEN APPLIED 5CHA TO CHAIN *B*. 5CHA

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Components

#1: Protein/peptide ALPHA-CHYMOTRYPSIN A


Mass: 1253.511 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P00766, chymotrypsin
#2: Protein ALPHA-CHYMOTRYPSIN A


Mass: 13934.556 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P00766, chymotrypsin
#3: Protein ALPHA-CHYMOTRYPSIN A


Mass: 10074.495 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P00766, chymotrypsin
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 247 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.12 Å3/Da / Density % sol: 42.04 %
Crystal grow
*PLUS
pH: 4.2 / Method: unknown
Components of the solutions
*PLUS
Conc.: 50 %sat / Common name: ammonium sulfate

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Data collection

RadiationScattering type: x-ray
Radiation wavelengthRelative weight: 1
Reflection
*PLUS
Num. obs: 26342 / % possible obs: 70 % / Num. measured all: 37693

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Processing

RefinementHighest resolution: 1.67 Å
Refinement stepCycle: LAST / Highest resolution: 1.67 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3472 0 0 247 3719

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