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- PDB-3it9: Crystal structure of Penicillin-Binding Protein 6 (PBP6) from E. ... -

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Basic information

Entry
Database: PDB / ID: 3it9
TitleCrystal structure of Penicillin-Binding Protein 6 (PBP6) from E. coli in apo state
ComponentsD-alanyl-D-alanine carboxypeptidase dacC
KeywordsHYDROLASE / Penicillin-Binding Protein / PBP6 / DD-carboxypeptidase / peptidoglycan / Carboxypeptidase / Cell inner membrane / Cell membrane / Cell shape / Cell wall biogenesis/degradation / Membrane / Peptidoglycan synthesis / Protease
Function / homology
Function and homology information


serine-type D-Ala-D-Ala carboxypeptidase / serine-type D-Ala-D-Ala carboxypeptidase activity / penicillin binding / peptidoglycan biosynthetic process / carboxypeptidase activity / cell wall organization / outer membrane-bounded periplasmic space / regulation of cell shape / response to xenobiotic stimulus / protein homodimerization activity ...serine-type D-Ala-D-Ala carboxypeptidase / serine-type D-Ala-D-Ala carboxypeptidase activity / penicillin binding / peptidoglycan biosynthetic process / carboxypeptidase activity / cell wall organization / outer membrane-bounded periplasmic space / regulation of cell shape / response to xenobiotic stimulus / protein homodimerization activity / proteolysis / plasma membrane
Similarity search - Function
Peptidoglycan synthesis regulatory factor (PBP3), Domain 2 / D-Ala-D-Ala carboxypeptidase, C-terminal domain / D-Ala-D-Ala carboxypeptidase, C-terminal domain superfamily / Peptidase S11, D-Ala-D-Ala carboxypeptidase A, C-terminal / Penicillin-binding protein 5, C-terminal domain / Penicillin-binding protein 5, C-terminal domain / Penicillin-binding protein, C-terminal domain superfamily / Peptidase S11, D-alanyl-D-alanine carboxypeptidase A, N-terminal / Peptidase S11, D-alanyl-D-alanine carboxypeptidase A / D-alanyl-D-alanine carboxypeptidase ...Peptidoglycan synthesis regulatory factor (PBP3), Domain 2 / D-Ala-D-Ala carboxypeptidase, C-terminal domain / D-Ala-D-Ala carboxypeptidase, C-terminal domain superfamily / Peptidase S11, D-Ala-D-Ala carboxypeptidase A, C-terminal / Penicillin-binding protein 5, C-terminal domain / Penicillin-binding protein 5, C-terminal domain / Penicillin-binding protein, C-terminal domain superfamily / Peptidase S11, D-alanyl-D-alanine carboxypeptidase A, N-terminal / Peptidase S11, D-alanyl-D-alanine carboxypeptidase A / D-alanyl-D-alanine carboxypeptidase / Beta-lactamase / DD-peptidase/beta-lactamase superfamily / Beta-lactamase/transpeptidase-like / Sandwich / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
sucrose / D-alanyl-D-alanine carboxypeptidase DacC
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å
AuthorsChen, Y. / Zhang, W. / Shi, Q. / Hesek, D. / Lee, M. / Mobashery, S. / Shoichet, B.K.
CitationJournal: J.Am.Chem.Soc. / Year: 2009
Title: Crystal structures of penicillin-binding protein 6 from Escherichia coli.
Authors: Chen, Y. / Zhang, W. / Shi, Q. / Hesek, D. / Lee, M. / Mobashery, S. / Shoichet, B.K.
History
DepositionAug 27, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 20, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 1, 2017Group: Refinement description / Category: software
Item: _software.classification / _software.contact_author ..._software.classification / _software.contact_author / _software.contact_author_email / _software.date / _software.language / _software.location / _software.name / _software.type / _software.version
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations / Non-polymer description / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / entity_name_com / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_molecule_features / pdbx_nonpoly_scheme / struct_asym / struct_conn / struct_ref_seq_dif / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.src_method / _entity.type / _struct_asym.entity_id / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Sep 6, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: D-alanyl-D-alanine carboxypeptidase dacC
B: D-alanyl-D-alanine carboxypeptidase dacC
C: D-alanyl-D-alanine carboxypeptidase dacC
D: D-alanyl-D-alanine carboxypeptidase dacC
hetero molecules


Theoretical massNumber of molelcules
Total (without water)153,81814
Polymers152,3654
Non-polymers1,45310
Water7,584421
1
A: D-alanyl-D-alanine carboxypeptidase dacC
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,9685
Polymers38,0911
Non-polymers8774
Water181
TypeNameSymmetry operationNumber
crystal symmetry operation2_545-x,y-1/2,-z1
2
B: D-alanyl-D-alanine carboxypeptidase dacC
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,2833
Polymers38,0911
Non-polymers1922
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: D-alanyl-D-alanine carboxypeptidase dacC
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,1872
Polymers38,0911
Non-polymers961
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: D-alanyl-D-alanine carboxypeptidase dacC
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,3794
Polymers38,0911
Non-polymers2883
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)56.949, 184.853, 81.610
Angle α, β, γ (deg.)90.000, 100.620, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11D
21A
12B
22D
13C
23D
14A
24B
15C
25A
35D

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDRefine codeAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111ASNASNILEILE3DD187 - 189187 - 189
211ASNASNILEILE3AA187 - 189187 - 189
121GLUGLUPHEPHE3DD183 - 184183 - 184
221GLUGLUPHEPHE3AA183 - 184183 - 184
112ASNASNGLYGLY3BB333 - 334333 - 334
212ASNASNGLYGLY3DD333 - 334333 - 334
113LEULEUGLYGLY5CC332 - 334332 - 334
213LEULEUGLYGLY5DD332 - 334332 - 334
114GLUGLUPHEPHE3AA183 - 184183 - 184
214GLUGLUPHEPHE3BB183 - 184183 - 184
115GLUGLUALAALA3CC290 - 291290 - 291
215GLUGLUALAALA3AA290 - 291290 - 291
315GLUGLUALAALA3DD290 - 291290 - 291

NCS ensembles :
ID
1
2
3
4
5

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Components

#1: Protein
D-alanyl-D-alanine carboxypeptidase dacC / DD-carboxypeptidase / DD-peptidase / Penicillin-binding protein 6 / PBP-6


Mass: 38091.301 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: DACC / Plasmid: PET-24a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: P08506, serine-type D-Ala-D-Ala carboxypeptidase
#2: Polysaccharide beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose / sucrose /


Type: oligosaccharide, Oligosaccharide / Class: Nutrient / Mass: 342.297 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: oligosaccharide with reducing-end-to-reducing-end glycosidic bond
References: sucrose
DescriptorTypeProgram
DFrufb2-1DGlcpaGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,2,1/[ha122h-2b_2-5][a2122h-1a_1-5]/1-2/a2-b1WURCSPDB2Glycan 1.1.0
[][b-D-Fruf]{[(2+1)][a-D-Glcp]{}}LINUCSPDB-CARE
#3: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: SO4
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 421 / 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: 2.77 Å3/Da / Density % sol: 55.61 %
Crystal growTemperature: 292 K / pH: 4.5
Details: PEG 8000, pH 4.5, vapor diffusion, hanging drop, temperature 292K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.3.1 / Wavelength: 1.11587
DetectorType: ADSC QUANTUM Q315R / Detector: CCD / Date: May 3, 2008 / Details: MIRRORS
RadiationMonochromator: DOUBLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Scattering type: x-ray
Radiation wavelengthWavelength: 1.11587 Å / Relative weight: 1
ReflectionResolution: 2.1→50 Å / Num. obs: 93487 / % possible obs: 97.7 % / Redundancy: 2.5 % / Rmerge(I) obs: 0.062 / Net I/σ(I): 12.3
Reflection shellResolution: 2.1→2.18 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.481 / % possible all: 97

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
REFMACrefinement
PDB_EXTRACT3.005data extraction
HKL-2000data collection
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: model constructed by Modeller using 1NZO

1nzo


Resolution: 2.1→50 Å / Cor.coef. Fo:Fc: 0.954 / Cor.coef. Fo:Fc free: 0.931 / Occupancy max: 1 / Occupancy min: 0.4 / SU B: 6.07 / SU ML: 0.158 / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.224 / ESU R Free: 0.198 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE
RfactorNum. reflection% reflectionSelection details
Rfree0.259 4673 5 %RANDOM
Rwork0.207 ---
obs0.21 93444 97.2 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 40.19 Å2
Baniso -1Baniso -2Baniso -3
1-2.15 Å20 Å20.09 Å2
2---2.1 Å20 Å2
3----0.01 Å2
Refinement stepCycle: LAST / Resolution: 2.1→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10637 0 86 421 11144
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.02210907
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg0.8581.97314785
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg13.22651403
X-RAY DIFFRACTIONr_dihedral_angle_2_deg38.40824.922447
X-RAY DIFFRACTIONr_dihedral_angle_3_deg22.503151905
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.1961557
X-RAY DIFFRACTIONr_chiral_restr0.0850.21696
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.0218080
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_it1.5951.56907
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it2.762211095
X-RAY DIFFRACTIONr_scbond_it4.23434000
X-RAY DIFFRACTIONr_scangle_it6.5474.53686
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11D20tight positional0.10.05
21B8tight positional0.250.05
41A8tight positional0.10.05
51C8tight positional0.090.05
52A8tight positional0.070.05
53D8tight positional0.040.05
31C8medium positional0.230.5
12A25loose positional0.415
22D4loose positional0.895
32D4loose positional1.135
42B12loose positional1.285
51C6loose positional0.795
52A6loose positional0.465
53D6loose positional0.75
11D20tight thermal1.940.5
21B8tight thermal0.90.5
41A8tight thermal1.110.5
51C8tight thermal0.940.5
52A8tight thermal0.340.5
53D8tight thermal0.780.5
31C8medium thermal1.832
12A25loose thermal2.0810
22D4loose thermal1.4210
32D4loose thermal1.9910
42B12loose thermal1.1210
51C6loose thermal0.4310
52A6loose thermal0.5210
53D6loose thermal0.5510
LS refinement shellResolution: 2.1→2.15 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.38 320 -
Rwork0.301 6049 -
obs--90.58 %

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