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- PDB-1sub: CALCIUM-INDEPENDENT SUBTILISIN BY DESIGN -

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Basic information

Entry
Database: PDB / ID: 1sub
TitleCALCIUM-INDEPENDENT SUBTILISIN BY DESIGN
ComponentsSUBTILISIN BPN' CRB-S3
KeywordsHYDROLASE(SERINE PROTEINASE)
Function / homology
Function and homology information


subtilisin / sporulation resulting in formation of a cellular spore / fibrinolysis / serine-type endopeptidase activity / proteolysis / extracellular region / metal ion binding
Similarity search - Function
: / Fervidolysin N-terminal prodomain / Subtilisin Carlsberg-like catalytic domain / Peptidase S8 propeptide/proteinase inhibitor I9 superfamily / Peptidase S8/S53 domain / Peptidase S8, subtilisin, His-active site / : / Serine proteases, subtilase family, histidine active site. / Serine proteases, subtilase family, aspartic acid active site. / Peptidase S8, subtilisin, Asp-active site ...: / Fervidolysin N-terminal prodomain / Subtilisin Carlsberg-like catalytic domain / Peptidase S8 propeptide/proteinase inhibitor I9 superfamily / Peptidase S8/S53 domain / Peptidase S8, subtilisin, His-active site / : / Serine proteases, subtilase family, histidine active site. / Serine proteases, subtilase family, aspartic acid active site. / Peptidase S8, subtilisin, Asp-active site / Serine proteases, subtilase family, serine active site. / Peptidase S8, subtilisin, Ser-active site / Peptidase S8, subtilisin-related / Serine proteases, subtilase domain profile. / Peptidase S8/S53 domain superfamily / Subtilase family / Peptidase S8/S53 domain / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
ACETONE / : / Subtilisin BPN'
Similarity search - Component
Biological speciesBacillus amyloliquefaciens (bacteria)
MethodX-RAY DIFFRACTION / Resolution: 1.75 Å
AuthorsGallagher, T. / Bryan, P. / Gilliland, G.L.
CitationJournal: Proteins / Year: 1993
Title: Calcium-independent subtilisin by design.
Authors: Gallagher, T. / Bryan, P. / Gilliland, G.L.
History
DepositionJun 10, 1992Processing site: BNL
Revision 1.0Jan 31, 1994Provider: repository / Type: Initial release
Revision 1.1Mar 3, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site
Revision 1.4Nov 3, 2021Group: Database references / Derived calculations
Category: database_2 / struct_conn ...database_2 / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.5Oct 9, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature
Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: SUBTILISIN BPN' CRB-S3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,7114
Polymers27,5741
Non-polymers1373
Water2,738152
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)41.770, 79.520, 37.220
Angle α, β, γ (deg.)90.00, 114.97, 90.00
Int Tables number4
Space group name H-MP1211
Atom site foot note1: RESIDUE PRO 168 IS A CIS PROLINE.
2: RESIDUE CYS 221 (REPLACING THE CATALYTIC SER 221) IS OXIDIZED TO A SULFONYL (TWO OXYGENS BOUND TO SG). THESE ADDUCTS ARE INCLUDED AS *HETATM* RECORDS REFERRED TO HET GROUP *CYA*, RESIDUE NUMBER ...2: RESIDUE CYS 221 (REPLACING THE CATALYTIC SER 221) IS OXIDIZED TO A SULFONYL (TWO OXYGENS BOUND TO SG). THESE ADDUCTS ARE INCLUDED AS *HETATM* RECORDS REFERRED TO HET GROUP *CYA*, RESIDUE NUMBER 278. CONECT RECORDS SPECIFY BONDING.
3: RESIDUE CA 295 IS THE 'A' SITE CALCIUM. RESIDUE K 297 IS THE 'B' SITE MONOVALENT SUBSITE.

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Components

#1: Protein SUBTILISIN BPN' CRB-S3


Mass: 27573.564 Da / Num. of mol.: 1 / Mutation: N218S, SER221CSD
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus amyloliquefaciens (bacteria) / References: UniProt: P00782, subtilisin
#2: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Ca
#3: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: K
#4: Chemical ChemComp-ACN / ACETONE


Mass: 58.079 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H6O
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 152 / Source method: isolated from a natural source / Formula: H2O
Compound detailsSECONDARY STRUCTURE ASSIGNMENT IS ACCORDING TO KABSCH AND SANDER (BIOPOLYMERS 22, 2577-2637, 1983).
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: 2.03 Å3/Da / Density % sol: 39.51 %
Crystal grow
*PLUS
pH: 9 / Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDDetails
155 %acetone1reservoir
250 mMglycine-NaOH1droppH9.0

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Data collection

RadiationScattering type: x-ray
Radiation wavelengthRelative weight: 1

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Processing

SoftwareName: PROFFT / Classification: refinement
RefinementResolution: 1.75→10 Å / σ(F): 1 /
RfactorNum. reflection
obs0.148 19514
Refinement stepCycle: LAST / Resolution: 1.75→10 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1938 0 2 156 2096
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONp_bond_d0.0170.024
X-RAY DIFFRACTIONp_angle_d0.0380.035
X-RAY DIFFRACTIONp_angle_deg
X-RAY DIFFRACTIONp_planar_d0.0360.04
X-RAY DIFFRACTIONp_hb_or_metal_coord
X-RAY DIFFRACTIONp_mcbond_it
X-RAY DIFFRACTIONp_mcangle_it
X-RAY DIFFRACTIONp_scbond_it
X-RAY DIFFRACTIONp_scangle_it
X-RAY DIFFRACTIONp_plane_restr0.0330.03
X-RAY DIFFRACTIONp_chiral_restr0.2820.25
X-RAY DIFFRACTIONp_singtor_nbd0.3710.2
X-RAY DIFFRACTIONp_multtor_nbd0.1230.2
X-RAY DIFFRACTIONp_xhyhbond_nbd0.1690.2
X-RAY DIFFRACTIONp_xyhbond_nbd
X-RAY DIFFRACTIONp_planar_tor53
X-RAY DIFFRACTIONp_staggered_tor16.715
X-RAY DIFFRACTIONp_orthonormal_tor28.220
X-RAY DIFFRACTIONp_transverse_tor
X-RAY DIFFRACTIONp_special_tor
Software
*PLUS
Name: PROFFT / Classification: refinement
Refinement
*PLUS
Highest resolution: 1.75 Å / Lowest resolution: 10 Å / Num. reflection obs: 19514 / σ(F): 1 / Rfactor obs: 0.148
Solvent computation
*PLUS
Displacement parameters
*PLUS

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