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- PDB-9d7a: OXA-58-NA-1-157 5 min complex -

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Open data


ID or keywords:

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Basic information

Entry
Database: PDB / ID: 9d7a
TitleOXA-58-NA-1-157 5 min complex
Components(Beta-lactamase) x 2
KeywordsHYDROLASE/INHIBITOR / beta-lactamase / carbapenemase / antibiotic resistance / inhibitor / HYDROLASE / HYDROLASE-INHIBITOR complex
Function / homology
Function and homology information


penicillin binding / antibiotic catabolic process / cell wall organization / beta-lactamase / beta-lactamase activity / response to antibiotic / plasma membrane
Similarity search - Function
Beta-lactamase, class-D active site / Beta-lactamase class-D active site. / : / Penicillin-binding protein, transpeptidase / Penicillin binding protein transpeptidase domain / Beta-lactamase/transpeptidase-like / Prokaryotic membrane lipoprotein lipid attachment site profile.
Similarity search - Domain/homology
Chem-Y33 / Beta-lactamase OXA-58
Similarity search - Component
Biological speciesAcinetobacter baumannii (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2.05 Å
AuthorsSmith, C.A. / Maggiolo, A.O. / Toth, M. / Vakulenko, S.B.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)1R01AI155723 United States
CitationJournal: Acs Infect Dis. / Year: 2024
Title: Decarboxylation of the Catalytic Lysine Residue by the C5 alpha-Methyl-Substituted Carbapenem NA-1-157 Leads to Potent Inhibition of the OXA-58 Carbapenemase.
Authors: Toth, M. / Stewart, N.K. / Maggiolo, A.O. / Quan, P. / Khan, M.M.K. / Buynak, J.D. / Smith, C.A. / Vakulenko, S.B.
History
DepositionAug 16, 2024Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 11, 2024Provider: repository / Type: Initial release
Revision 1.1Dec 25, 2024Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Beta-lactamase
B: Beta-lactamase
C: Beta-lactamase
D: Beta-lactamase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)127,5568
Polymers125,9504
Non-polymers1,6064
Water1,53185
1
A: Beta-lactamase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,9002
Polymers31,4981
Non-polymers4011
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Beta-lactamase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,9002
Polymers31,4981
Non-polymers4011
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: Beta-lactamase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,9002
Polymers31,4981
Non-polymers4011
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: Beta-lactamase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,8572
Polymers31,4551
Non-polymers4011
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)37.065, 66.257, 193.061
Angle α, β, γ (deg.)90.00, 91.12, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein Beta-lactamase


Mass: 31498.209 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Acinetobacter baumannii (bacteria)
Gene: blaOXA-58, bla-oxa-58, bla-oxa58, GSE42_20550, P9867_20895
Production host: Escherichia coli (E. coli) / References: UniProt: Q2TR58, beta-lactamase
#2: Protein Beta-lactamase


Mass: 31455.205 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Acinetobacter baumannii (bacteria)
Gene: blaOXA-58, bla-oxa-58, bla-oxa58, GSE42_20550, P9867_20895
Production host: Escherichia coli (E. coli) / References: UniProt: Q2TR58, beta-lactamase
#3: Chemical
ChemComp-Y33 / (5R)-3-{[(3S,5S)-5-(dimethylcarbamoyl)pyrrolidin-3-yl]sulfanyl}-5-[(2S,3R)-3-hydroxy-1-oxobutan-2-yl]-5-methyl-4,5-dihydro-1H-pyrrole-2-carboxylic acid


Mass: 401.478 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C17H27N3O6S / Feature type: SUBJECT OF INVESTIGATION
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 85 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
Has protein modificationY

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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: 2.15 Å3/Da / Density % sol: 42.75 %
Crystal growTemperature: 289 K / Method: vapor diffusion, sitting drop
Details: 0.2 M sodium acetate, 0.1 M Tris-HCl pH 8.5, 30% PEG4000

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL12-2 / Wavelength: 0.9795 Å
DetectorType: DECTRIS EIGER2 XE 16M / Detector: PIXEL / Date: May 18, 2024
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.05→39.01 Å / Num. obs: 58348 / % possible obs: 99.1 % / Redundancy: 7.1 % / CC1/2: 0.996 / Rpim(I) all: 0.063 / Rrim(I) all: 0.168 / Net I/σ(I): 7.3
Reflection shellResolution: 2.05→2.11 Å / Mean I/σ(I) obs: 1.5 / Num. unique obs: 4506 / CC1/2: 0.665 / Rpim(I) all: 0.523

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Processing

Software
NameVersionClassification
PHENIX(1.21.1_5286: ???)refinement
XDSdata reduction
Aimlessdata scaling
MOLREPphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS / Resolution: 2.05→39.01 Å / SU ML: 0.34 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 32.5 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2926 2809 4.82 %
Rwork0.2397 --
obs0.2423 58264 98.85 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.05→39.01 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7882 0 0 85 7967
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0088087
X-RAY DIFFRACTIONf_angle_d1.08910956
X-RAY DIFFRACTIONf_dihedral_angle_d18.9173011
X-RAY DIFFRACTIONf_chiral_restr0.0551181
X-RAY DIFFRACTIONf_plane_restr0.0071417
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.05-2.090.3771350.33682760X-RAY DIFFRACTION99
2.09-2.120.35891500.29262737X-RAY DIFFRACTION99
2.12-2.160.34641650.27262799X-RAY DIFFRACTION100
2.16-2.210.3011260.26662734X-RAY DIFFRACTION99
2.21-2.260.31461300.26612749X-RAY DIFFRACTION100
2.26-2.310.33761460.27022796X-RAY DIFFRACTION99
2.31-2.370.30371260.26012747X-RAY DIFFRACTION99
2.37-2.430.32381230.26342765X-RAY DIFFRACTION99
2.43-2.50.31951320.26072727X-RAY DIFFRACTION98
2.5-2.580.42071230.2612749X-RAY DIFFRACTION98
2.58-2.670.34331610.25642776X-RAY DIFFRACTION100
2.67-2.780.29931320.25062785X-RAY DIFFRACTION100
2.78-2.910.3141380.24922827X-RAY DIFFRACTION100
2.91-3.060.28941490.26222783X-RAY DIFFRACTION100
3.06-3.250.31191330.2642732X-RAY DIFFRACTION98
3.25-3.50.29271580.23942751X-RAY DIFFRACTION98
3.5-3.860.27041460.22572748X-RAY DIFFRACTION97
3.86-4.410.261310.20922820X-RAY DIFFRACTION99
4.41-5.560.25891570.20882809X-RAY DIFFRACTION99
5.56-39.010.24411480.20952861X-RAY DIFFRACTION98
Refinement TLS params.

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

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
10.53760.52520.27150.53440.02110.79790.1037-0.4779-0.5650.12480.0192-0.0564-0.01270.5867-0.00050.2999-0.04-0.01140.66150.06460.43553.999-4.78281.798
21.77760.02750.2865-0.25290.1375-0.1024-0.03360.02780.2076-0.095-0.0669-0.0812-0.27520.17-0.00030.36460.0141-0.00880.40520.02790.3256-5.2331.66563.731
30.1391-0.0865-0.24320.48510.34460.52180.22940.7424-1.325-0.0343-0.009-0.173-0.1964-0.46380.03340.3605-0.0221-0.02920.6006-0.20720.6578-12.151-13.99853.029
42.4359-0.54560.60930.9215-0.84442.51540.08110.4112-0.1392-0.0044-0.09490.0016-0.2133-0.0272-0.00020.32310.00030.00960.3136-0.03360.29-7.111.22561.409
51.08681.0067-0.12291.2693-0.14830.86090.0372-0.2694-1.05160.2673-0.5760.32390.23860.2038-0.04680.3698-0.0479-0.00990.4602-0.05030.4094-2.235-5.95972.534
60.1778-0.16460.14340.20840.0630.99750.3345-0.2638-0.59930.1317-0.3347-0.141-0.2092-0.7995-0.04140.3615-0.10550.02170.50160.15530.4592-6.057-8.92880.197
70.4513-0.54820.22670.5882-0.15210.2989-0.03410.4810.0457-0.35810.12510.37460.2246-0.12550.00070.3603-0.0251-0.0420.38010.0260.3191-3.761-33.6811.863
80.5611-0.1535-0.35520.8231-0.01060.241-0.0016-0.14310.2037-0.0921-0.16790.2444-0.1314-0.2069-0.00020.2534-0.0085-0.02460.34330.0290.3405-1.88-26.54322.701
90.685-0.7659-0.39990.7791-0.0890.84640.0801-0.6226-0.20340.0088-0.065-0.12470.2029-0.0425-00.4235-0.0274-0.03220.45250.04830.402914.127-33.20242.138
101.33980.47920.53460.8278-0.32611.8776-0.1502-0.4159-0.01550.04640.12080.05920.0137-0.09010.00010.3688-0.01980.03090.3421-0.02370.36816.295-27.06540.006
110.63820.00670.35790.01440.04570.11150.0154-0.37330.65240.11080.00930.1905-0.1742-0.04180.00450.3559-0.03070.01220.1633-0.02790.25839.193-20.05625.078
120.68620.31480.54260.80521.26491.6681-0.11240.254-0.30850.03760.257-0.26090.0890.5227-00.3065-0.005-0.01070.3302-0.00920.398510.544-31.83125.304
130.7817-0.05150.16080.76110.14650.7351-0.24110.6225-0.4713-0.2393-0.1522-0.36080.08210.1024-0.0070.2949-0.05950.09570.43220.05980.52275.338-29.87118.645
140.3164-0.04130.25530.5005-0.18790.2826-0.01330.1371-0.3186-0.21860.0036-0.04340.17530.0956-0.00050.3199-0.0224-0.05160.3969-0.07040.41444.059-39.47216.616
151.08540.7762-0.17270.7349-0.39931.533-0.1622-0.5372-0.11090.35560.13310.3043-0.8672-0.0973-0.03920.38160.0002-0.01840.6403-0.04360.352712.2534.50435.38
160.52450.15780.33070.77320.27170.5507-0.12790.201-0.0046-0.1322-0.06420.38510.1439-0.3325-0.01790.2537-0.08740.02980.31620.01670.348614.64-1.00623.178
171.5176-0.3477-0.03950.6138-0.62820.4642-0.32160.22570.5535-0.07780.1069-0.4234-0.00660.05700.433-0.0347-0.07550.37790.03720.390130.2179.956.491
181.8799-0.1525-0.38061.1980.62972.3533-0.04670.14010.0517-0.138-0.01870.07990.00090.0265-0.00010.2925-0.0081-0.01940.19190.02040.25723.490.12814.473
190.78580.2318-1.03950.7914-0.45561.2562-0.499-0.77420.71730.51080.1684-0.35340.04310.0353-0.01570.292-0.0137-0.0450.3080.00660.401321.4091.67328.038
200.43790.2876-0.21350.3153-0.48560.9556-0.0024-0.08770.35720.6543-0.286-0.1368-0.51940.4823-0.02040.3933-0.0064-0.0420.3705-0.13530.359620.07210.75731.195
211.17370.11490.60070.23320.42430.704-0.09840.98840.7888-0.35650.05770.3951-0.02540.883-0.00490.48750.09340.01220.77430.19870.480620.17426.47162.947
220.41410.2744-0.03170.38650.66570.6336-0.2409-0.1081-0.05620.35290.1693-0.18170.43020.3886-0.00030.31580.01820.06980.3606-0.05210.292115.80423.82579.09
232.53431.45060.43980.95640.58181.3969-0.1933-1.0010.7143-0.7018-0.72970.1387-0.4348-0.3114-0.28490.5465-0.014-0.00170.8144-0.14890.52062.7640.27993.675
240.070.08840.10490.14480.09180.1969-0.15950.81580.5683-0.6584-0.51730.1396-0.7040.0539-0.01020.4965-0.04280.06550.559-0.05150.62512.01540.00387.114
252.20990.20790.09881.489-0.06152.09420.00440.030.23210.0951-0.03690.10620.2597-0.2420.00020.3313-0.00980.04860.4067-0.05420.36129.54626.71584.847
260.7104-0.3901-0.65510.86620.01910.7239-0.62830.87170.5208-0.9420.53780.02960.12160.2529-0.00430.3584-0.0292-0.01210.41790.07690.394111.72226.04571.169
271.0680.0713-0.11081.33951.34971.47430.06461.14051.3567-1.2337-0.62020.1828-1.1636-0.5043-0.12640.45540.0339-0.1050.72350.28330.541113.03634.65866.54
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 38:60 )A38 - 60
2X-RAY DIFFRACTION2( CHAIN A AND RESID 61:105 )A61 - 105
3X-RAY DIFFRACTION3( CHAIN A AND RESID 106:131 )A106 - 131
4X-RAY DIFFRACTION4( CHAIN A AND RESID 132:239 )A132 - 239
5X-RAY DIFFRACTION5( CHAIN A AND RESID 240:261 )A240 - 261
6X-RAY DIFFRACTION6( CHAIN A AND RESID 262:280 )A262 - 280
7X-RAY DIFFRACTION7( CHAIN B AND RESID 38:60 )B38 - 60
8X-RAY DIFFRACTION8( CHAIN B AND RESID 61:86 )B61 - 86
9X-RAY DIFFRACTION9( CHAIN B AND RESID 87:117 )B87 - 117
10X-RAY DIFFRACTION10( CHAIN B AND RESID 118:177 )B118 - 177
11X-RAY DIFFRACTION11( CHAIN B AND RESID 178:196 )B178 - 196
12X-RAY DIFFRACTION12( CHAIN B AND RESID 197:239 )B197 - 239
13X-RAY DIFFRACTION13( CHAIN B AND RESID 240:254 )B240 - 254
14X-RAY DIFFRACTION14( CHAIN B AND RESID 255:280 )B255 - 280
15X-RAY DIFFRACTION15( CHAIN C AND RESID 38:60 )C38 - 60
16X-RAY DIFFRACTION16( CHAIN C AND RESID 61:87 )C61 - 87
17X-RAY DIFFRACTION17( CHAIN C AND RESID 88:131 )C88 - 131
18X-RAY DIFFRACTION18( CHAIN C AND RESID 132:239 )C132 - 239
19X-RAY DIFFRACTION19( CHAIN C AND RESID 240:254 )C240 - 254
20X-RAY DIFFRACTION20( CHAIN C AND RESID 255:280 )C255 - 280
21X-RAY DIFFRACTION21( CHAIN D AND RESID 36:60 )D36 - 60
22X-RAY DIFFRACTION22( CHAIN D AND RESID 61:95 )D61 - 95
23X-RAY DIFFRACTION23( CHAIN D AND RESID 96:117 )D96 - 117
24X-RAY DIFFRACTION24( CHAIN D AND RESID 118:131 )D118 - 131
25X-RAY DIFFRACTION25( CHAIN D AND RESID 132:239 )D132 - 239
26X-RAY DIFFRACTION26( CHAIN D AND RESID 243:254 )D243 - 254
27X-RAY DIFFRACTION27( CHAIN D AND RESID 255:280 )D255 - 280

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