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- PDB-5idu: Crystal structure of an acyl-CoA dehydrogenase domain protein fro... -

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Basic information

Entry
Database: PDB / ID: 5idu
TitleCrystal structure of an acyl-CoA dehydrogenase domain protein from Burkholderia phymatum bound to FAD
ComponentsAcyl-CoA dehydrogenase domain protein
KeywordsOXIDOREDUCTASE / NIAID / structural genomics / FAD / tetramer / Seattle Structural Genomics Center for Infectious Disease / SSGCID
Function / homology
Function and homology information


acyl-CoA dehydrogenase activity / flavin adenine dinucleotide binding
Similarity search - Function
Acyl-CoA dehydrogenases signature 1. / Acyl-CoA dehydrogenase, conserved site / Butyryl-Coa Dehydrogenase, subunit A; domain 1 / Acyl-CoA dehydrogenase/oxidase, N-terminal domain / Butyryl-CoA Dehydrogenase, subunit A, domain 2 / Butyryl-CoA Dehydrogenase, subunit A; domain 2 / Acyl-CoA dehydrogenase/oxidase C-terminal / Acyl-CoA dehydrogenase/oxidase, N-terminal / Acyl-CoA dehydrogenase, N-terminal domain / Acyl-CoA dehydrogenase, C-terminal domain ...Acyl-CoA dehydrogenases signature 1. / Acyl-CoA dehydrogenase, conserved site / Butyryl-Coa Dehydrogenase, subunit A; domain 1 / Acyl-CoA dehydrogenase/oxidase, N-terminal domain / Butyryl-CoA Dehydrogenase, subunit A, domain 2 / Butyryl-CoA Dehydrogenase, subunit A; domain 2 / Acyl-CoA dehydrogenase/oxidase C-terminal / Acyl-CoA dehydrogenase/oxidase, N-terminal / Acyl-CoA dehydrogenase, N-terminal domain / Acyl-CoA dehydrogenase, C-terminal domain / Acyl-CoA oxidase/dehydrogenase, middle domain / Acyl-CoA dehydrogenase, middle domain / Acyl-CoA dehydrogenase/oxidase, N-terminal domain superfamily / Butyryl-CoA Dehydrogenase, subunit A, domain 3 / Acyl-CoA oxidase/dehydrogenase, middle domain superfamily / Acyl-CoA dehydrogenase/oxidase, N-terminal and middle domain superfamily / Acyl-CoA dehydrogenase-like, C-terminal / Butyryl-CoA Dehydrogenase, subunit A; domain 3 / Up-down Bundle / Beta Barrel / Orthogonal Bundle / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
FLAVIN-ADENINE DINUCLEOTIDE / Acyl-CoA dehydrogenase domain protein
Similarity search - Component
Biological speciesBurkholderia phymatum (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.95 Å
AuthorsSeattle Structural Genomics Center for Infectious Disease (SSGCID) / Edwards, T.E.
CitationJournal: To Be Published
Title: Crystal structure of an acyl-CoA dehydrogenase domain protein from Burkholderia phymatum bound to FAD
Authors: Edwards, T.E. / Mayclin, S.J. / Seattle Structural Genomics Center for Infectious Disease (SSGCID)
History
DepositionFeb 24, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 9, 2016Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2016Group: Data collection
Revision 1.2Sep 27, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_oper_list.symmetry_operation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Acyl-CoA dehydrogenase domain protein
B: Acyl-CoA dehydrogenase domain protein
C: Acyl-CoA dehydrogenase domain protein
D: Acyl-CoA dehydrogenase domain protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)181,03819
Polymers177,2134
Non-polymers3,82515
Water21,4201189
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area24820 Å2
ΔGint-87 kcal/mol
Surface area51240 Å2
MethodPISA
Unit cell
Length a, b, c (Å)84.180, 108.420, 189.440
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein
Acyl-CoA dehydrogenase domain protein


Mass: 44303.180 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Burkholderia phymatum (bacteria) / Strain: DSM 17167 / STM815 / Gene: Bphy_4072 / Production host: Escherichia coli (E. coli) / References: UniProt: B2JPK4
#2: Chemical
ChemComp-FAD / FLAVIN-ADENINE DINUCLEOTIDE


Mass: 785.550 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C27H33N9O15P2 / Comment: FAD*YM
#3: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 11 / Source method: obtained synthetically / Formula: C2H6O2
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1189 / 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: 2.44 Å3/Da / Density % sol: 49.57 %
Crystal growTemperature: 289 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: BuphA.00027.f.B1.PS02558 at 21.1 mg/mL against Morepheus D6 10% PEG 8000, 20% ethylene glycol, 0.02 M each alcohol, 0.1 M MOPS/Hepes pH 7.5, crystal tracking ID 269543d6, unique puck ID evl4-1

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97872 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Feb 3, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97872 Å / Relative weight: 1
ReflectionResolution: 1.95→50 Å / Num. obs: 126600 / % possible obs: 99.9 % / Redundancy: 5 % / CC1/2: 0.997 / Rmerge(I) obs: 0.09 / Net I/σ(I): 10.1
Reflection shellResolution: 1.95→2 Å / Redundancy: 5 % / Rmerge(I) obs: 0.501 / Mean I/σ(I) obs: 3.33 / % possible all: 99.9

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Processing

Software
NameVersionClassification
PHENIX(dev_2313: ???)refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4L1F
Resolution: 1.95→47.36 Å / SU ML: 0.16 / Cross valid method: NONE / σ(F): 1.36 / Phase error: 17.73
RfactorNum. reflection% reflection
Rfree0.1896 2007 1.59 %
Rwork0.1537 --
obs0.1543 126592 99.89 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 1.95→47.36 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11806 0 256 1189 13251
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00612422
X-RAY DIFFRACTIONf_angle_d0.78316892
X-RAY DIFFRACTIONf_dihedral_angle_d14.2517230
X-RAY DIFFRACTIONf_chiral_restr0.0481873
X-RAY DIFFRACTIONf_plane_restr0.0052185
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.9501-1.99880.26371290.20538828X-RAY DIFFRACTION100
1.9988-2.05290.26331640.20128776X-RAY DIFFRACTION100
2.0529-2.11330.25341430.18598811X-RAY DIFFRACTION100
2.1133-2.18150.18981450.16968803X-RAY DIFFRACTION100
2.1815-2.25950.20381420.16248804X-RAY DIFFRACTION100
2.2595-2.34990.21051160.15218866X-RAY DIFFRACTION100
2.3499-2.45690.18841600.15158848X-RAY DIFFRACTION100
2.4569-2.58640.19551320.15168871X-RAY DIFFRACTION100
2.5864-2.74840.18991460.15468851X-RAY DIFFRACTION100
2.7484-2.96060.18181350.15158907X-RAY DIFFRACTION100
2.9606-3.25850.18171400.15648912X-RAY DIFFRACTION100
3.2585-3.72980.17621390.14928971X-RAY DIFFRACTION100
3.7298-4.69850.15461720.12619011X-RAY DIFFRACTION100
4.6985-47.37390.18261440.14859326X-RAY DIFFRACTION100
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)
11.2985-0.5895-0.39912.120.96331.7508-0.1160.1597-0.0894-0.01140.1566-0.40890.03820.2258-0.04890.0959-0.0008-0.00890.2243-0.04690.233545.4687-23.1081-24.7914
23.59291.56591.5082.43422.31922.2228-0.0330.6821-0.0636-0.55450.2106-0.1825-0.30530.3264-0.09910.1909-0.01670.05310.3847-0.09780.22738.532-35.9896-43.4612
30.94190.1506-0.14331.75140.49290.18270.0153-0.0128-0.17540.13220.1299-0.25950.04820.0903-0.12370.10340.0237-0.03650.1192-0.04260.184537.996-36.2978-26.9869
40.9840.30670.24631.0093-0.27431.15680.1372-0.0421-0.3457-0.00870.0432-0.11430.13650.079-0.12030.15480.0373-0.06540.0798-0.04320.200528.3819-47.2163-28.6116
51.08780.0343-0.11632.0789-0.25721.15120.0688-0.1185-0.18830.10730.12130.11720.2546-0.0101-0.15170.15760.0098-0.07520.09610.00420.159519.0697-51.569-29.5267
60.54760.16540.28511.08670.04690.24180.04050.0487-0.1439-0.01720.0652-0.0660.09160.0441-0.08610.11390.0206-0.01580.0968-0.02240.119925.9255-39.2908-32.1926
70.8696-0.06680.1020.5476-0.19511.2986-0.0340.05610.0326-0.04550.0586-0.07460.02330.0049-0.07130.0965-0.0152-0.02520.0929-0.0290.112431.7987-12.3843-27.5827
80.6949-0.01880.33940.6563-0.78752.25090.05010.0982-0.0483-0.0773-0.0028-0.02040.16270.1936-0.02530.10560.0071-0.01270.1039-0.02140.123825.4472-20.4495-34.8861
92.4037-0.0029-0.18092.72420.75186.3183-0.0245-0.3805-0.28380.34560.04950.01730.3044-0.098-0.04870.1592-0.007-0.03330.16920.06740.202715.9687-25.7352-11.1542
102.159-0.9666-0.86731.21420.97953.1878-0.04010.1822-0.0733-0.0636-0.07770.10990.0513-0.29830.14830.0926-0.0301-0.01850.07890.01430.1426-7.0165-12.2764-51.2071
117.6150.3001-2.08672.45061.27811.362-0.10.2364-0.9952-0.15740.1012-0.15810.48180.2265-0.0180.26830.0106-0.00430.1978-0.0440.2510.31-22.5245-63.1946
121.01880.4884-0.81480.3533-0.00681.93730.03230.35120.1924-0.036-0.07550.0248-0.0782-0.14030.0140.12440.0081-0.0150.18210.04190.11910.9859-7.4304-59.6653
130.76550.04-0.23841.0817-0.49331.11960.03810.31330.167-0.0725-0.095-0.1262-0.06590.19090.05230.14950.01040.01060.24380.07560.143220.5263-3.6357-65.5873
140.8455-0.04-0.25290.9323-0.1041.42750.02950.33360.2886-0.4199-0.1135-0.2474-0.03650.22710.06820.19610.00080.03380.31880.12620.263624.94961.2874-70.9195
151.2970.8385-0.7592.26-1.78742.09220.00490.07850.1133-0.08650.07160.0654-0.0691-0.0406-0.09790.11310.0043-0.00940.0990.00190.09328.2887-10.4963-48.0256
160.5651-0.48220.30911.6567-0.53760.5843-0.0243-0.0427-0.064-0.03650.0341-0.01580.0853-0.02390.02270.08730.00440.00460.08750.0050.12032.5625-15.5306-35.3535
170.7217-0.66620.2371.6447-0.21710.31690.03050.150.0743-0.1862-0.05-0.08280.01250.06170.02580.1056-0.0007-0.00040.13350.01920.107512.7832-14.1791-42.8539
182.7692-0.5542-0.70265.57321.85563.8858-0.08630.26790.2763-0.32430.12090.1186-0.3314-0.0406-0.00830.1738-0.0411-0.01650.21350.08790.169715.04428.5934-40.1076
191.5738-1.02221.45781.5618-1.86082.8888-0.08850.02770.11720.04960.11470.0637-0.2635-0.012-0.05630.18860.0055-0.01980.1197-0.00410.1534-8.28839.9106-45.0953
201.43290.0737-1.03031.51590.51146.57310.2028-0.39030.42420.27590.0032-0.1072-0.85210.3972-0.18150.3484-0.02290.05840.1721-0.02390.2644-10.091515.1919-19.0872
211.4259-0.4137-1.30920.8115-0.3412.03370.0453-0.2014-0.06710.10050.08180.1134-0.3064-0.0993-0.11390.16670.03220.03510.15340.03820.1476-15.41835.2674-21.8839
220.76840.224-0.07740.55710.07511.2824-0.0437-1.237-0.50820.27630.0460.0131-0.0451-0.062-0.00840.24660.00790.05810.61720.31390.3071-17.8345-5.4475-4.6725
232.0652-0.18260.49060.1556-0.29171.0373-0.1048-0.0538-0.5553-0.35240.0664-0.01870.163-0.2914-0.04260.25070.05670.12720.23770.12490.4199-19.0937-10.9624-16.207
241.4937-0.06820.38960.5871-0.01820.6825-0.0152-0.14440.11670.0462-0.0002-0.0234-0.11280.02060.00810.12390.00810.00280.10580.02020.10126.30923.2038-28.5448
252.53752.01610.87213.91660.62141.07270.1245-0.7415-0.00580.0827-0.24070.3466-0.0395-0.18780.12280.28620.00510.00640.5165-0.0110.28735.01173.484-15.5493
263.00990.42080.53515.35192.3995.63710.1613-0.1506-0.36060.1126-0.09190.24130.11-0.4291-0.03430.08810.01430.01090.15560.09290.1904-4.4811-20.7101-29.2546
270.7551-0.2687-0.06982.671.65272.19240.0224-0.16-0.07630.32940.0371-0.0040.25250.0125-0.07520.2171-0.0024-0.04010.19480.02290.101233.0236-14.5105-0.0004
281.3273-1.4883-0.14345.4310.58822.03260.0297-0.2463-0.0248-0.1354-0.04190.5191-0.5893-0.54290.14480.32560.09580.00080.3518-0.07230.159423.96065.9497.3974
291.35240.03470.33321.1204-0.09641.5186-0.10250.010.40630.0263-0.0059-0.0944-0.60010.29510.06990.3624-0.0904-0.02990.2359-0.03420.220836.783711.3728-5.2362
301.14490.06510.49041.00510.1011.51210.0236-0.1420.19340.118-0.03940.0377-0.327-0.0235-0.0050.21090.00690.0010.0963-0.01550.108825.4873-0.5484-10.7273
313.17320.1537-1.17490.7951-0.30873.06490.0934-0.34120.30580.09870.05380.0137-0.41750.0367-0.05060.2112-0.02-0.05490.15990.00930.197326.1602-0.2691-18.9969
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 6 through 35 )
2X-RAY DIFFRACTION2chain 'A' and (resid 36 through 57 )
3X-RAY DIFFRACTION3chain 'A' and (resid 58 through 113 )
4X-RAY DIFFRACTION4chain 'A' and (resid 114 through 151 )
5X-RAY DIFFRACTION5chain 'A' and (resid 152 through 192 )
6X-RAY DIFFRACTION6chain 'A' and (resid 193 through 277 )
7X-RAY DIFFRACTION7chain 'A' and (resid 278 through 322 )
8X-RAY DIFFRACTION8chain 'A' and (resid 323 through 375 )
9X-RAY DIFFRACTION9chain 'A' and (resid 376 through 397 )
10X-RAY DIFFRACTION10chain 'B' and (resid 6 through 35 )
11X-RAY DIFFRACTION11chain 'B' and (resid 36 through 57 )
12X-RAY DIFFRACTION12chain 'B' and (resid 58 through 93 )
13X-RAY DIFFRACTION13chain 'B' and (resid 94 through 219 )
14X-RAY DIFFRACTION14chain 'B' and (resid 220 through 240 )
15X-RAY DIFFRACTION15chain 'B' and (resid 241 through 277 )
16X-RAY DIFFRACTION16chain 'B' and (resid 278 through 318 )
17X-RAY DIFFRACTION17chain 'B' and (resid 319 through 375 )
18X-RAY DIFFRACTION18chain 'B' and (resid 376 through 394 )
19X-RAY DIFFRACTION19chain 'C' and (resid -7 through 18 )
20X-RAY DIFFRACTION20chain 'C' and (resid 19 through 57 )
21X-RAY DIFFRACTION21chain 'C' and (resid 58 through 113 )
22X-RAY DIFFRACTION22chain 'C' and (resid 114 through 233 )
23X-RAY DIFFRACTION23chain 'C' and (resid 234 through 252 )
24X-RAY DIFFRACTION24chain 'C' and (resid 253 through 353 )
25X-RAY DIFFRACTION25chain 'C' and (resid 354 through 375 )
26X-RAY DIFFRACTION26chain 'C' and (resid 376 through 397 )
27X-RAY DIFFRACTION27chain 'D' and (resid 6 through 35 )
28X-RAY DIFFRACTION28chain 'D' and (resid 36 through 58 )
29X-RAY DIFFRACTION29chain 'D' and (resid 59 through 192 )
30X-RAY DIFFRACTION30chain 'D' and (resid 193 through 353 )
31X-RAY DIFFRACTION31chain 'D' and (resid 354 through 397 )

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