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- PDB-1chg: CHYMOTRYPSINOGEN,2.5 ANGSTROMS CRYSTAL STRUCTURE, COMPARISON WITH... -

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Entry
Database: PDB / ID: 1chg
TitleCHYMOTRYPSINOGEN,2.5 ANGSTROMS CRYSTAL STRUCTURE, COMPARISON WITH ALPHA-CHYMOTRYPSIN,AND IMPLICATIONS FOR ZYMOGEN ACTIVATION
ComponentsCHYMOTRYPSINOGEN A
KeywordsHYDROLASE ZYMOGEN (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 / Serine proteases, trypsin family, histidine active site. / Peptidase S1A, chymotrypsin family / 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 / Serine proteases, trypsin family, histidine active site. / Peptidase S1A, chymotrypsin family / 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 (domestic cattle)
MethodX-RAY DIFFRACTION / Resolution: 2.5 Å
AuthorsFreer, S.T. / Kraut, J. / Robertus, J.D. / Wright, H.T. / Xuong, N.H.
Citation
Journal: Biochemistry / Year: 1970
Title: Chymotrypsinogen: 2.5-angstrom crystal structure, comparison with alpha-chymotrypsin, and implications for zymogen activation.
Authors: Freer, S.T. / Kraut, J. / Robertus, J.D. / Wright, H.T. / Xuong, N.H.
#1: Journal: The Enzymes,Third Edition / Year: 1971
Title: Chymotrypsinogen,X-Ray Structure
Authors: Kraut, J.
#2: Journal: J.Mol.Biol. / Year: 1973
Title: Comparison of the Crystal Structures of Chymotrypsinogen-A and Alpha-Chymotrypsin
Authors: Wright, H.T.
#3: Journal: J.Mol.Biol. / Year: 1973
Title: Activation of Chymotrypsinogen-A,an Hypothesis Based Upon Comparison of the Crystal Structures of Chymotrypsinogen-A and Alpha-Chymotrypsin
Authors: Wright, H.T.
#4: Journal: Atlas of Macromolecular Structure on Microfiche / Year: 1976
#5: Journal: Atlas of Protein Sequence and Structure (Data Section)
Year: 1972
History
DepositionMar 1, 1975Processing site: BNL
Revision 1.0Nov 22, 1976Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 2.0Sep 27, 2023Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Other
Category: atom_site / atom_sites ...atom_site / atom_sites / chem_comp_atom / chem_comp_bond / database_2 / database_PDB_matrix / pdbx_database_status / pdbx_validate_main_chain_plane / pdbx_validate_planes / pdbx_validate_polymer_linkage / pdbx_validate_rmsd_angle / pdbx_validate_rmsd_bond / pdbx_validate_symm_contact / pdbx_validate_torsion / struct_conn
Item: _atom_site.Cartn_x / _atom_site.Cartn_y ..._atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_sites.fract_transf_matrix[1][1] / _atom_sites.fract_transf_matrix[1][2] / _atom_sites.fract_transf_matrix[1][3] / _atom_sites.fract_transf_matrix[2][1] / _atom_sites.fract_transf_matrix[2][2] / _atom_sites.fract_transf_matrix[2][3] / _atom_sites.fract_transf_matrix[3][1] / _atom_sites.fract_transf_matrix[3][2] / _atom_sites.fract_transf_matrix[3][3] / _atom_sites.fract_transf_vector[1] / _atom_sites.fract_transf_vector[2] / _atom_sites.fract_transf_vector[3] / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _database_PDB_matrix.origx[1][1] / _database_PDB_matrix.origx[1][2] / _database_PDB_matrix.origx[1][3] / _database_PDB_matrix.origx[2][1] / _database_PDB_matrix.origx[2][2] / _database_PDB_matrix.origx[2][3] / _database_PDB_matrix.origx[3][1] / _database_PDB_matrix.origx[3][2] / _database_PDB_matrix.origx[3][3] / _database_PDB_matrix.origx_vector[1] / _database_PDB_matrix.origx_vector[2] / _database_PDB_matrix.origx_vector[3] / _pdbx_database_status.process_site / _pdbx_validate_main_chain_plane.improper_torsion_angle / _pdbx_validate_planes.rmsd / _pdbx_validate_symm_contact.dist / _pdbx_validate_torsion.auth_comp_id / _pdbx_validate_torsion.auth_seq_id / _pdbx_validate_torsion.phi / _pdbx_validate_torsion.psi / _struct_conn.pdbx_dist_value
Details: Coordinates and associated ncs operations (if present) transformed into standard crystal frame
Provider: repository / Type: Remediation
Revision 2.1Oct 23, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: CHYMOTRYPSINOGEN A


Theoretical massNumber of molelcules
Total (without water)25,6861
Polymers25,6861
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)52.000, 63.900, 77.100
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein CHYMOTRYPSINOGEN A


Mass: 25686.037 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bos taurus (domestic cattle) / References: UniProt: P00766
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: 2.49 Å3/Da / Density % sol: 50.65 %
Crystal grow
*PLUS
pH: 6.3 / Method: microdialysis
Components of the solutions
*PLUS
IDCommon nameCrystal-IDSol-IDDetails
1chymotrypsinogen11150mg
2water110.5ml

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Data collection

RadiationScattering type: x-ray
Radiation wavelengthRelative weight: 1

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Processing

RefinementRfactor Rwork: 0.43 / Highest resolution: 2.5 Å
Refinement stepCycle: LAST / Highest resolution: 2.5 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1643 0 0 0 1643

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