[English] 日本語
Yorodumi
- PDB-9cd8: Crystal Structure of Acetyl-CoA synthetase from Cryptococcus neof... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 9cd8
TitleCrystal Structure of Acetyl-CoA synthetase from Cryptococcus neoformans H99 in complex with inhibitor HGN-1310 (dd3-027)
Components(Acetyl-coenzyme A ...) x 2
KeywordsLIGASE / SSGCID / STRUCTURAL GENOMICS / SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE / Acetyl-coenzyme A synthetase 2
Function / homology
Function and homology information


acetate-CoA ligase / acetate-CoA ligase activity / acetyl-CoA biosynthetic process from acetate / AMP binding / ATP binding / metal ion binding / cytosol
Similarity search - Function
Acetate-CoA ligase / Acetyl-coenzyme A synthetase, N-terminal domain / Acetyl-coenzyme A synthetase N-terminus / ANL, N-terminal domain / AMP-binding enzyme C-terminal domain / AMP-binding enzyme, C-terminal domain / AMP-binding, conserved site / Putative AMP-binding domain signature. / AMP-dependent synthetase/ligase / AMP-binding enzyme / AMP-binding enzyme, C-terminal domain superfamily
Similarity search - Domain/homology
: / Acetyl-coenzyme A synthetase
Similarity search - Component
Biological speciesCryptococcus neoformans var. grubii (Cryptococcus neoformans serotype A)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsSeattle Structural Genomics Center for Infectious Disease / Seattle Structural Genomics Center for Infectious Disease (SSGCID)
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)75N93022C00036 United States
National Institutes of Health/Office of the DirectorS10OD030394 United States
CitationJournal: Nat Commun / Year: 2025
Title: Discovery and mechanism of a highly selective, antifungal acetyl-CoA synthetase inhibitor.
Authors: Jezewski, A.J. / Alden, K.M. / Propp, J. / Daraji, D.G. / Lail 3rd, C.L. / Heene, M.E. / Fuller, A.J. / Ferreira, J.C. / Liu, L. / Battaile, K.P. / Williams, N.S. / Staker, B.L. / Lovell, S. ...Authors: Jezewski, A.J. / Alden, K.M. / Propp, J. / Daraji, D.G. / Lail 3rd, C.L. / Heene, M.E. / Fuller, A.J. / Ferreira, J.C. / Liu, L. / Battaile, K.P. / Williams, N.S. / Staker, B.L. / Lovell, S. / Hagen, T.J. / Krysan, D.J.
History
DepositionJun 24, 2024Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 29, 2025Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Acetyl-coenzyme A synthetase
B: Acetyl-coenzyme A synthetase
C: Acetyl-coenzyme A synthetase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)234,96320
Polymers232,4683
Non-polymers2,49517
Water9,872548
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8150 Å2
ΔGint-82 kcal/mol
Surface area65400 Å2
MethodPISA
Unit cell
Length a, b, c (Å)176.224, 176.224, 159.461
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number92
Space group name H-MP41212
Components on special symmetry positions
IDModelComponents
11B-828-

HOH

-
Components

-
Acetyl-coenzyme A ... , 2 types, 3 molecules ABC

#1: Protein Acetyl-coenzyme A synthetase


Mass: 77516.781 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: The ALY modified LYS residues was modeled in chain A only.
Source: (gene. exp.) Cryptococcus neoformans var. grubii (Cryptococcus neoformans serotype A)
Gene: CNAG_00797 / Plasmid: CrneC.00629.a.FS11 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: J9VFT1, acetate-CoA ligase
#2: Protein Acetyl-coenzyme A synthetase


Mass: 77475.750 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Cryptococcus neoformans var. grubii (Cryptococcus neoformans serotype A)
Gene: CNAG_00797 / Plasmid: CrneC.00629.a.FS11 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: J9VFT1, acetate-CoA ligase

-
Non-polymers , 5 types, 565 molecules

#3: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: C3H8O3
#4: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: SO4
#5: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#6: Chemical ChemComp-A1AV1 / (5P)-3-azido-N-[(5-cyclopropyl-1,2-oxazol-3-yl)methyl]-5-(2,3-dihydro-1-benzofuran-5-yl)-N-methylbenzamide


Mass: 415.445 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C23H21N5O3 / Feature type: SUBJECT OF INVESTIGATION
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 548 / Source method: isolated from a natural source / Formula: H2O

-
Details

Has ligand of interestY
Has protein modificationY

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 2.66 Å3/Da / Density % sol: 53.81 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: Index F8: 0.2 M Ammonium sulfate, 0.1 M HEPES pH 7.5, 25% w/v Polyethylene glycol 3,350. CrneC.00629.a.FS11.PD00460 at 10 mg/mL. 2mM HGN-1310 (dd3-027) inhibitor added to the protein prior ...Details: Index F8: 0.2 M Ammonium sulfate, 0.1 M HEPES pH 7.5, 25% w/v Polyethylene glycol 3,350. CrneC.00629.a.FS11.PD00460 at 10 mg/mL. 2mM HGN-1310 (dd3-027) inhibitor added to the protein prior to crystallization. Plate: 13756 well F8 drop 2. Puck: PSL-1509, Cryo: 20% glycerol + 80% crystallant

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: NSLS-II / Beamline: 19-ID / Wavelength: 0.9786 Å
DetectorType: DECTRIS EIGER2 XE 9M / Detector: PIXEL / Date: Nov 19, 2023
RadiationMonochromator: Double Crystal Si 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9786 Å / Relative weight: 1
ReflectionResolution: 2.4→176.22 Å / Num. obs: 98167 / % possible obs: 100 % / Redundancy: 13 % / CC1/2: 0.998 / Rmerge(I) obs: 0.177 / Rpim(I) all: 0.051 / Rrim(I) all: 0.184 / Χ2: 1 / Net I/σ(I): 13 / Num. measured all: 1273162
Reflection shellResolution: 2.4→2.46 Å / % possible obs: 100 % / Redundancy: 13.5 % / Rmerge(I) obs: 1.854 / Num. measured all: 96895 / Num. unique obs: 7166 / CC1/2: 0.663 / Rpim(I) all: 0.523 / Rrim(I) all: 1.927 / Χ2: 0.99 / Net I/σ(I) obs: 1.7

-
Processing

Software
NameVersionClassification
PHENIX1.21rc1_5177refinement
Aimlessdata scaling
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.4→124.61 Å / SU ML: 0.31 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 20.79 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2192 4864 4.96 %
Rwork0.1785 --
obs0.1805 98069 99.99 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.4→124.61 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14436 0 159 548 15143
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00315056
X-RAY DIFFRACTIONf_angle_d0.60320506
X-RAY DIFFRACTIONf_dihedral_angle_d12.5415432
X-RAY DIFFRACTIONf_chiral_restr0.0462182
X-RAY DIFFRACTIONf_plane_restr0.0062647
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.4-2.430.35171620.29953078X-RAY DIFFRACTION100
2.43-2.460.3311530.28083042X-RAY DIFFRACTION100
2.46-2.490.32631530.25643106X-RAY DIFFRACTION100
2.49-2.520.31841710.24213023X-RAY DIFFRACTION100
2.52-2.550.27091780.22763072X-RAY DIFFRACTION100
2.55-2.590.261600.21833044X-RAY DIFFRACTION100
2.59-2.620.26911570.20963078X-RAY DIFFRACTION100
2.62-2.660.26761470.19993085X-RAY DIFFRACTION100
2.66-2.70.27841490.19713095X-RAY DIFFRACTION100
2.7-2.750.23581510.20583074X-RAY DIFFRACTION100
2.75-2.790.25721530.20953100X-RAY DIFFRACTION100
2.79-2.850.24661790.20863065X-RAY DIFFRACTION100
2.85-2.90.24551640.22283079X-RAY DIFFRACTION100
2.9-2.960.26411650.23763055X-RAY DIFFRACTION100
2.96-3.020.28581460.243098X-RAY DIFFRACTION100
3.02-3.090.28581690.22523077X-RAY DIFFRACTION100
3.09-3.170.2511510.2063108X-RAY DIFFRACTION100
3.17-3.260.20641750.18883094X-RAY DIFFRACTION100
3.26-3.350.2011600.17593087X-RAY DIFFRACTION100
3.35-3.460.23171480.17833115X-RAY DIFFRACTION100
3.46-3.580.22871560.1773087X-RAY DIFFRACTION100
3.59-3.730.2321560.18423124X-RAY DIFFRACTION100
3.73-3.90.21961740.16723127X-RAY DIFFRACTION100
3.9-4.10.17761840.14443092X-RAY DIFFRACTION100
4.1-4.360.1541550.12883121X-RAY DIFFRACTION100
4.36-4.70.16231380.12583173X-RAY DIFFRACTION100
4.7-5.170.17021570.12483180X-RAY DIFFRACTION100
5.17-5.920.19622050.1493136X-RAY DIFFRACTION100
5.92-7.460.18371520.17923230X-RAY DIFFRACTION100
7.46-124.610.22761960.18753360X-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)
11.9424-0.26910.19422.3498-0.03472.08150.04730.06490.2235-0.34890.0588-0.2812-0.18710.2046-0.09580.4807-0.05310.10290.38030.05070.3803-48.498234.2079-55.8537
20.7933-0.1842-0.11691.16070.01521.3234-0.0359-0.1319-0.06730.1220.09280.09180.0342-0.1252-0.05440.30270.01540.00580.31650.03910.3424-58.399111.4751-29.9849
30.6357-0.26950.07791.6058-0.46031.4818-0.0131-0.01470.0482-0.12440.16520.1483-0.2175-0.1909-0.14720.30880.01590.00350.30970.03250.3134-62.068427.1987-43.1301
41.7915-0.76010.91371.8794-1.01061.0279-0.02720.19390.1291-0.34080.13130.21120.0271-0.0624-0.10510.4825-0.0335-0.07270.4570.03610.4105-69.057225.2631-64.3552
53.87490.5569-0.24892.85860.16934.6327-0.04640.5098-0.4931-0.29560.0160.62310.7822-0.499-0.01990.7249-0.1116-0.17870.51620.05140.6699-79.230221.2706-64.6856
62.0773-0.19371.49231.5650.53973.68-0.1951-0.05070.30040.23820.0773-0.2447-0.19910.37480.10770.3682-0.0011-0.00140.426-0.00130.4118-22.137215.7351-6.4617
70.8938-0.2869-0.02271.078-0.2741.0926-0.1274-0.1688-0.18280.13040.15930.05910.1221-0.0119-0.03240.39590.08050.0230.42570.05790.3683-38.2461-8.8971-8.2615
80.66950.06930.38461.30730.181.1871-0.1575-0.2134-0.07260.27220.1283-0.0280.06480.06310.02520.39280.12660.03570.43250.04260.3058-32.3337-6.0173-3.5081
92.08720.2239-0.37431.73640.48971.786-0.2341-0.6949-0.0480.57660.0926-0.07930.1416-0.04710.14560.6540.1602-0.05480.7370.0080.4604-23.0681.723516.7445
102.72790.34630.6021.22290.14221.9671-0.0745-0.25850.30820.19720.1532-0.0038-0.38070.0549-0.08910.50820.1318-0.00870.4885-0.040.3855-36.329917.37882.5615
110.039-0.20270.00921.42490.46122.0251-0.1043-0.44150.27540.34670.06730.1715-0.3154-0.62910.05070.56690.20490.05490.6296-0.02060.4496-47.726319.54236.8693
122.7416-0.95130.99923.9086-0.20444.8137-0.10860.0625-0.05360.1160.2669-0.9155-0.12850.7918-0.12810.3735-0.0180.02680.6598-0.14480.7344-5.3407-17.2854-51.1378
133.0284-2.1686-1.31323.03331.58642.20060.0848-0.15410.31820.06110.2067-0.56590.04250.37-0.29910.4225-0.0535-0.01620.4238-0.07120.5492-15.4965-7.7682-38.4203
140.6844-0.2216-0.07260.76040.28910.8181-0.0671-0.0079-0.15590.03670.1158-0.05640.17030.0457-0.05270.3605-0.01410.01460.2716-0.02810.3809-31.4962-22.7295-46.144
151.35360.66920.28552.0140.71122.96130.1482-0.7590.1781.1962-0.13070.15430.21720.0948-0.02041.3249-0.06140.08870.9736-0.10090.6036-31.1-55.7485-30.2012
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 15 through 62 )
2X-RAY DIFFRACTION2chain 'A' and (resid 63 through 278 )
3X-RAY DIFFRACTION3chain 'A' and (resid 279 through 462 )
4X-RAY DIFFRACTION4chain 'A' and (resid 463 through 629 )
5X-RAY DIFFRACTION5chain 'A' and (resid 630 through 677 )
6X-RAY DIFFRACTION6chain 'B' and (resid 24 through 84 )
7X-RAY DIFFRACTION7chain 'B' and (resid 85 through 245 )
8X-RAY DIFFRACTION8chain 'B' and (resid 246 through 382 )
9X-RAY DIFFRACTION9chain 'B' and (resid 383 through 432 )
10X-RAY DIFFRACTION10chain 'B' and (resid 433 through 507 )
11X-RAY DIFFRACTION11chain 'B' and (resid 508 through 562 )
12X-RAY DIFFRACTION12chain 'C' and (resid 3 through 47 )
13X-RAY DIFFRACTION13chain 'C' and (resid 48 through 84 )
14X-RAY DIFFRACTION14chain 'C' and (resid 85 through 551 )
15X-RAY DIFFRACTION15chain 'C' and (resid 552 through 677 )

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more