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- PDB-5lvs: Self-assembled protein-aromatic foldamer complexes with 2:3 and 2... -

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Basic information

Entry
Database: PDB / ID: 5lvs
TitleSelf-assembled protein-aromatic foldamer complexes with 2:3 and 2:2:1 stoichiometries
ComponentsCarbonic anhydrase 2
KeywordsLYASE / PROTEIN-FOLDAMER COMPLEX / PROTEIN FOLDAMER INTERACTIONS / MODIFIED INHIBITOR / ANCHORED FOLDAMER / HCAII DIMERISATION / QUINOLINE OLIGOAMIDE FOLDAMER / BENZENE SULFONAMIDE MODIFIED INHIBITOR / LYASE-LYASE INHIBITOR COMPLEX
Function / homology
Function and homology information


positive regulation of cellular pH reduction / positive regulation of dipeptide transmembrane transport / regulation of monoatomic anion transport / secretion / cyanamide hydratase / cyanamide hydratase activity / arylesterase activity / regulation of chloride transport / Reversible hydration of carbon dioxide / angiotensin-activated signaling pathway ...positive regulation of cellular pH reduction / positive regulation of dipeptide transmembrane transport / regulation of monoatomic anion transport / secretion / cyanamide hydratase / cyanamide hydratase activity / arylesterase activity / regulation of chloride transport / Reversible hydration of carbon dioxide / angiotensin-activated signaling pathway / positive regulation of synaptic transmission, GABAergic / regulation of intracellular pH / morphogenesis of an epithelium / carbonic anhydrase / carbonate dehydratase activity / carbon dioxide transport / Erythrocytes take up oxygen and release carbon dioxide / Erythrocytes take up carbon dioxide and release oxygen / neuron cellular homeostasis / one-carbon metabolic process / apical part of cell / myelin sheath / extracellular exosome / zinc ion binding / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Carbonic Anhydrase II / Alpha carbonic anhydrase / Carbonic anhydrase, alpha-class, conserved site / Alpha-carbonic anhydrases signature. / Carbonic anhydrase, alpha-class / Alpha carbonic anhydrase domain / Alpha carbonic anhydrase domain superfamily / Eukaryotic-type carbonic anhydrase / Alpha-carbonic anhydrases profile. / Eukaryotic-type carbonic anhydrase ...Carbonic Anhydrase II / Alpha carbonic anhydrase / Carbonic anhydrase, alpha-class, conserved site / Alpha-carbonic anhydrases signature. / Carbonic anhydrase, alpha-class / Alpha carbonic anhydrase domain / Alpha carbonic anhydrase domain superfamily / Eukaryotic-type carbonic anhydrase / Alpha-carbonic anhydrases profile. / Eukaryotic-type carbonic anhydrase / Roll / Alpha Beta
Similarity search - Domain/homology
Chem-6H0 / FORMYL GROUP / Chem-QUJ / Chem-QUK / Chem-QVE / 8-azanyl-4-oxidanyl-quinoline-2-carboxylic acid / Carbonic anhydrase 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.42 Å
AuthorsJewginski, M. / LANGLOIS D'ESTAINTOT, B. / Granier, T. / Huc, Y.
Funding support Poland, 1items
OrganizationGrant numberCountry
Polish Ministry of Science and Higher Education (Mobility Plus Program) Poland
CitationJournal: J. Am. Chem. Soc. / Year: 2017
Title: Self-Assembled Protein-Aromatic Foldamer Complexes with 2:3 and 2:2:1 Stoichiometries.
Authors: Jewginski, M. / Granier, T. / Langlois d'Estaintot, B. / Fischer, L. / Mackereth, C.D. / Huc, I.
History
DepositionSep 14, 2016Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 8, 2017Provider: repository / Type: Initial release
Revision 1.1Mar 15, 2017Group: Database references
Revision 1.2Jun 12, 2019Group: Data collection / Structure summary
Category: audit_author / database_PDB_rev / database_PDB_rev_record
Item: _audit_author.name
Revision 2.0Nov 15, 2023Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations / Refinement description
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp_atom / chem_comp_bond / database_2 / struct_conn / struct_conn_type / struct_ncs_dom_lim
Item: _atom_site.auth_atom_id / _atom_site.label_atom_id ..._atom_site.auth_atom_id / _atom_site.label_atom_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_label_atom_id / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _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_asym_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_type.id / _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
Revision 2.1Jan 17, 2024Group: Refinement description / Category: pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Carbonic anhydrase 2
B: Carbonic anhydrase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)63,41231
Polymers58,3162
Non-polymers5,09629
Water10,359575
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4740 Å2
ΔGint-17 kcal/mol
Surface area22720 Å2
MethodPISA
Unit cell
Length a, b, c (Å)158.730, 54.810, 84.700
Angle α, β, γ (deg.)90.000, 112.770, 90.000
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B

NCS domain segments:

Component-ID: 0 / Ens-ID: 1 / Beg auth comp-ID: SER / Beg label comp-ID: SER / End auth comp-ID: LYS / End label comp-ID: LYS / Refine code: 0 / Auth seq-ID: 2 - 260 / Label seq-ID: 1 - 259

Dom-IDAuth asym-IDLabel asym-ID
1AA
2BB

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein Carbonic anhydrase 2 / / Carbonate dehydratase II / Carbonic anhydrase C / CAC / Carbonic anhydrase II / CA-II


Mass: 29157.863 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CA2 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P00918, carbonic anhydrase

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Non-polymers , 9 types, 604 molecules

#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#3: Chemical ChemComp-6H0 / ~{N}-[[3-(4-formamidobutoxy)phenyl]methyl]-4-sulfamoyl-benzamide


Mass: 405.468 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C19H23N3O5S
#4: Chemical
ChemComp-QUK / 8-azanyl-4-(3-azanylpropoxy)quinoline-2-carboxylic acid


Mass: 261.276 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C13H15N3O3
#5: Chemical ChemComp-QVS / 8-azanyl-4-oxidanyl-quinoline-2-carboxylic acid


Mass: 204.182 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H8N2O3
#6: Chemical ChemComp-QVE / 8-azanyl-4-(2-hydroxy-2-oxoethyloxy)quinoline-2-carboxylic acid


Mass: 262.218 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C12H10N2O5
#7: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C3H8O3
#8: Chemical
ChemComp-QUJ / 8-azanyl-4-(2-methylpropoxy)quinoline-2-carboxylic acid


Mass: 260.288 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C14H16N2O3
#9: Chemical ChemComp-FOR / FORMYL GROUP / Aldehyde


Mass: 30.026 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: CH2O
#10: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 575 / 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: 2.91 Å3/Da / Density % sol: 57.77 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.3
Details: Ammonium sulfate 200 mM Sodium acetate 100 mM PEG 4000 24% NaN3 3 mM
PH range: 5.2 - 5.35

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 2 / Wavelength: 0.97625 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Jul 1, 2016 / Details: Kirkpatrick-Baez pair of bi-morph mirrors
RadiationMonochromator: channel cut cryogenically cooled monochromator crystal
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97625 Å / Relative weight: 1
ReflectionResolution: 1.42→50 Å / Num. obs: 125435 / % possible obs: 98.9 % / Observed criterion σ(I): -3 / Redundancy: 13.7 % / Biso Wilson estimate: 27.422 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.061 / Net I/σ(I): 24.17
Reflection shell
Resolution (Å)Highest resolution (Å)Rmerge(I) obsMean I/σ(I) obsCC1/2Diffraction-ID% possible all
1.42-1.461.3642.320.82197.7
1.46-1.51.0393.220.865197.9
1.5-1.560.7634.670.92198.2
1.56-1.60.5566.580.947198.4
1.6-1.70.3799.560.976198.6
1.7-1.80.23315.490.992198.8
1.8-20.12324.770.998199.2
2-2.50.06538.870.999199.6
2.5-30.04847.060.999199.8
3-40.04158.640.999199.8
4-60.04164.090.999199.8
6-100.04362.630.999199.8
100.05157.30.996197.1

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Processing

Software
NameVersionClassification
XSCALEdata scaling
REFMAC5.8.0155refinement
PDB_EXTRACT3.2data extraction
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3KS3

3ks3


Resolution: 1.42→45.85 Å / Cor.coef. Fo:Fc: 0.978 / Cor.coef. Fo:Fc free: 0.971 / SU B: 3.053 / SU ML: 0.049 / SU R Cruickshank DPI: 0.0568 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.057 / ESU R Free: 0.053
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED
RfactorNum. reflection% reflectionSelection details
Rfree0.1782 6182 4.9 %RANDOM
Rwork0.1494 ---
obs0.1509 119253 99 %-
Solvent computationIon probe radii: 0.7 Å / Shrinkage radii: 0.7 Å / VDW probe radii: 1.1 Å
Displacement parametersBiso max: 94.94 Å2 / Biso mean: 27.484 Å2 / Biso min: 11.31 Å2
Baniso -1Baniso -2Baniso -3
1--2.91 Å20 Å21.2 Å2
2---2.71 Å2-0 Å2
3---3.41 Å2
Refinement stepCycle: final / Resolution: 1.42→45.85 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4066 0 336 575 4977
Biso mean--30.47 41.11 -
Num. residues----518
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0140.0194641
X-RAY DIFFRACTIONr_bond_other_d0.0030.024210
X-RAY DIFFRACTIONr_angle_refined_deg1.852.0156331
X-RAY DIFFRACTIONr_angle_other_deg1.0153.0069702
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.4175545
X-RAY DIFFRACTIONr_dihedral_angle_2_deg32.98724.479192
X-RAY DIFFRACTIONr_dihedral_angle_3_deg11.05815688
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.6461515
X-RAY DIFFRACTIONr_chiral_restr0.1050.2640
X-RAY DIFFRACTIONr_gen_planes_refined0.010.0215273
X-RAY DIFFRACTIONr_gen_planes_other0.0030.021078
X-RAY DIFFRACTIONr_mcbond_it1.9142.2842144
X-RAY DIFFRACTIONr_mcbond_other1.9032.2762127
X-RAY DIFFRACTIONr_mcangle_it2.3393.4352673
X-RAY DIFFRACTIONr_rigid_bond_restr2.77338845
X-RAY DIFFRACTIONr_sphericity_free29.4915365
X-RAY DIFFRACTIONr_sphericity_bonded19.15858903
Refine LS restraints NCS

Ens-ID: 1 / Number: 17620 / Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Rms dev position: 0.06 Å / Weight position: 0.05

Dom-IDAuth asym-ID
1A
2B
LS refinement shellResolution: 1.42→1.457 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.474 455 -
Rwork0.462 8638 -
all-9093 -
obs--97.66 %
Refinement TLS params.

Method: refined / Origin x: 0 Å / Origin y: 0 Å / Origin z: 0 Å / 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)
10.07610.01980.01290.04340.00170.00930.0079-0.0159-0.0003-0.0107-0.0094-0.03730.0055-0.01390.00160.03170.00380.01140.02620.00460.0363
20.0294-0.0018-0.00550.0405-0.00170.0486-0.0023-0.0131-0.00020.01430.0014-0.01060.00160.01540.00080.04350.0015-0.00440.05040.00010.0028
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A2 - 305
2X-RAY DIFFRACTION2B2 - 305

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