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- PDB-2wwt: Intracellular subtilisin precursor from B. clausii -

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Basic information

Entry
Database: PDB / ID: 2wwt
TitleIntracellular subtilisin precursor from B. clausii
ComponentsINTRACELLULAR SUBTILISIN PROTEASE
KeywordsHYDROLASE / INTRACELLULAR PROTEINASE REGULATION
Function / homology
Function and homology information


serine-type endopeptidase activity / proteolysis / identical protein binding / metal ion binding
Similarity search - Function
Subtilisin Carlsberg-like catalytic domain / 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 / Serine proteases, subtilase domain profile. / Peptidase S8, subtilisin-related ...Subtilisin Carlsberg-like catalytic domain / 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 / Serine proteases, subtilase domain profile. / Peptidase S8, subtilisin-related / Peptidase S8/S53 domain superfamily / Subtilase family / Peptidase S8/S53 domain / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Intracellular subtilisin protease
Similarity search - Component
Biological speciesBACILLUS CLAUSII (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.68 Å
AuthorsVevodova, J. / Gamble, M. / Ariza, A. / Dodson, E. / Jones, D.D. / Wilson, K.S.
CitationJournal: Structure / Year: 2010
Title: Crystal Structure of an Intracellular Subtilisin Reveals Novel Structural Features Unique to This Subtilisin Family.
Authors: Vevodova, J. / Gamble, M. / Kunze, G. / Ariza, A. / Dodson, E. / Jones, D.D. / Wilson, K.S.
History
DepositionOct 27, 2009Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 8, 2010Provider: repository / Type: Initial release
Revision 1.1Nov 27, 2013Group: Refinement description / Source and taxonomy / Version format compliance
Revision 1.2Oct 7, 2015Group: Source and taxonomy
Revision 1.3Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: INTRACELLULAR SUBTILISIN PROTEASE
B: INTRACELLULAR SUBTILISIN PROTEASE
C: INTRACELLULAR SUBTILISIN PROTEASE
D: INTRACELLULAR SUBTILISIN PROTEASE
E: INTRACELLULAR SUBTILISIN PROTEASE
F: INTRACELLULAR SUBTILISIN PROTEASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)209,77911
Polymers209,6646
Non-polymers1155
Water36020
1
A: INTRACELLULAR SUBTILISIN PROTEASE
B: INTRACELLULAR SUBTILISIN PROTEASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,9113
Polymers69,8882
Non-polymers231
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3140 Å2
ΔGint-28.4 kcal/mol
Surface area20920 Å2
MethodPISA
2
E: INTRACELLULAR SUBTILISIN PROTEASE
F: INTRACELLULAR SUBTILISIN PROTEASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,9344
Polymers69,8882
Non-polymers462
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3320 Å2
ΔGint-38.5 kcal/mol
Surface area21340 Å2
MethodPISA
3
C: INTRACELLULAR SUBTILISIN PROTEASE
D: INTRACELLULAR SUBTILISIN PROTEASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)69,9344
Polymers69,8882
Non-polymers462
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3290 Å2
ΔGint-36.7 kcal/mol
Surface area21310 Å2
MethodPISA
Unit cell
Length a, b, c (Å)121.640, 121.640, 106.201
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number144
Space group name H-MP31
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(-0.6384, 0.7692, -0.0278), (0.7697, 0.6383, -0.0101), (0.01, -0.0279, -0.9996)7.3848, -2.949, 65.1895
2given(0.7311, 0.6822, -0.003), (0.6822, -0.731, 0.0136), (0.0071, -0.012, -0.9999)57.2641, -41.6108, 31.1338
3given(0.013, 0.9996, -0.0251), (-0.9996, 0.0136, 0.0237), (0.0241, 0.0248, 0.9994)60.677, -34.4581, -34.069
4given(0.7282, -0.6828, 0.0587), (0.6852, 0.7273, -0.0405), (-0.0151, 0.0697, 0.9975)-68.9449, 33.2229, -4.0509
5given(-0.9944, 0.1021, -0.0263), (0.1024, 0.9947, -0.0093), (0.0252, -0.012, -0.9996)-59.4228, 34.4761, 60.4674

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Components

#1: Protein
INTRACELLULAR SUBTILISIN PROTEASE


Mass: 34944.020 Da / Num. of mol.: 6 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) BACILLUS CLAUSII (bacteria)
Description: ISOLATED FROM A NOVOZYMES STRAIN OF B. CLAUSII. STRAIN NUMBER AVAILABLE ON REQUEST.
Plasmid: PET22B / Production host: ESCHERICHIA COLI BL21 (bacteria) / References: UniProt: D0AB41, subtilisin
#2: Chemical
ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Na
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 20 / Source method: isolated from a natural source / Formula: H2O
Compound detailsENGINEERED RESIDUE IN CHAIN A, SER 250 TO ALA ENGINEERED RESIDUE IN CHAIN B, SER 250 TO ALA ...ENGINEERED RESIDUE IN CHAIN A, SER 250 TO ALA ENGINEERED RESIDUE IN CHAIN B, SER 250 TO ALA ENGINEERED RESIDUE IN CHAIN C, SER 250 TO ALA ENGINEERED RESIDUE IN CHAIN D, SER 250 TO ALA ENGINEERED RESIDUE IN CHAIN E, SER 250 TO ALA ENGINEERED RESIDUE IN CHAIN F, SER 250 TO ALA

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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: 2.12 Å3/Da / Density % sol: 42 % / Description: NONE
Crystal growpH: 6.5
Details: 0.1M BISTRIS, PH6.5, 0.1 M NACL, 1.5M AMMONIUM SULFATE

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.9762
DetectorType: ADSC CCD / Detector: CCD / Date: Jul 25, 2006
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9762 Å / Relative weight: 1
Reflection twin
Crystal-IDIDOperatorDomain-IDFraction
11H, K, L10.72
11-H, H+K, -L20.28
ReflectionResolution: 2.68→60.8 Å / Num. obs: 49303 / % possible obs: 99.9 % / Observed criterion σ(I): 0 / Redundancy: 4 % / Rmerge(I) obs: 0.14 / Net I/σ(I): 11.6
Reflection shellResolution: 2.68→2.83 Å / Redundancy: 4.1 % / Rmerge(I) obs: 0.7 / Mean I/σ(I) obs: 2 / % possible all: 100

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Processing

Software
NameVersionClassification
MOSFLMdata reduction
SCALAdata scaling
MOLREPphasing
PHASERphasing
REFMAC5.5.0109refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1YJC

1yjc


Resolution: 2.68→105.57 Å / Cor.coef. Fo:Fc: 0.915 / Cor.coef. Fo:Fc free: 0.836 / SU B: 32.633 / SU ML: 0.288 / Cross valid method: THROUGHOUT / ESU R Free: 0.078 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.252 2484 5.1 %RANDOM
Rwork0.166 ---
obs0.17 46339 98.8 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 39.79 Å2
Baniso -1Baniso -2Baniso -3
1-5.03 Å20 Å20 Å2
2--5.03 Å20 Å2
3----10.07 Å2
Refinement stepCycle: LAST / Resolution: 2.68→105.57 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13285 0 5 20 13310
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0180.02213503
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.9051.95418349
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.80151787
X-RAY DIFFRACTIONr_dihedral_angle_2_deg42.54224.801554
X-RAY DIFFRACTIONr_dihedral_angle_3_deg22.719152082
X-RAY DIFFRACTIONr_dihedral_angle_4_deg21.0391565
X-RAY DIFFRACTIONr_chiral_restr0.120.22126
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.02110241
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.5631.58863
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.006214123
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it1.75434640
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it2.7014.54226
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.68→2.75 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.281 181 -
Rwork0.152 3397 -
obs--97.71 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
12.2786-0.8968-0.26982.32920.10151.12380.0133-0.0185-0.2289-0.033-0.05980.07020.01020.08250.04640.1781-0.0266-0.02550.24090.00020.016515.0448-20.433228.993
22.5047-0.70960.08782.41370.02241.7239-0.0565-0.045-0.31770.1833-0.0140.59570.0242-0.41140.07050.2484-0.01920.05170.3856-0.0360.2259-17.5785-6.008937.4463
31.70420.4052-0.31511.76780.10781.54510.0255-0.0310.09420.02590.05250.0489-0.10980.0894-0.0780.22290.01220.0340.1740.00280.030454.9741-17.3022.5957
42.08340.77080.3272.38350.38311.694-0.01810.2274-0.2356-0.06590.02090.17450.2299-0.1835-0.00280.2868-0.04370.00230.240.01390.125641.0753-49.9005-5.3357
53.86040.5526-0.33831.7399-0.21051.4333-0.11630.1932-0.2452-0.08020.113-0.22930.06890.29650.00330.27410.0090.00310.3856-0.05880.1134-44.159827.818223.1571
64.07970.4974-0.36821.9478-0.35791.1392-0.0503-0.0635-0.76010.1380.02210.15410.1726-0.29190.02820.3222-0.02310.00080.40980.00170.2887-77.609416.205832.6498
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A3 - 402
2X-RAY DIFFRACTION2B3 - 402
3X-RAY DIFFRACTION3C3 - 402
4X-RAY DIFFRACTION4D3 - 402
5X-RAY DIFFRACTION5E3 - 402
6X-RAY DIFFRACTION6F3 - 402

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