9UMG: VTC complex(Vtc5/Vtc4/Vtc3/Vtc1)
Cryo-EM structure of VTC complex(Vtc5/Vtc4/Vtc3/Vtc1). Determined by electron microscopy at 3.04 Å resolution. Released 21 Jan 2026.
- Method
- Electron microscopy
- Resolution
- 3.04 Å
- Organism
- Saccharomyces cerevisiae S288C
- Chains
- 6
- Atoms
- 9,877
- Mol. weight
- 180.75 kDa
- Ligands
- IHP
- Released
- 21 Jan 2026
Explore 9UMG in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9UMG contains 44 α-helices and 30 β-strands across 6 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
Chain A: 4 helices, 2 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-8 | 2 | 1 |
| β-strand | 17-18 | 2 | 1 |
| α-helix | 24-53 | 30 | |
| α-helix | 56-88 | 33 | |
| α-helix | 100-116 | 17 | |
| α-helix | 117-121 | 5 | |
Chain B: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 25-52 | 28 | |
| α-helix | 56-89 | 34 | |
| α-helix | 100-120 | 21 | |
Chain C: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 24-53 | 30 | |
| α-helix | 56-89 | 34 | |
| α-helix | 100-121 | 22 | |
Chain D: 16 helices, 15 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 197-203 | 7 | 2 |
| α-helix | 208-216 | 9 | |
| β-strand | 221-223 | 3 | 2 |
| β-strand | 236-243 | 8 | 2 |
| α-helix | 248-254 | 7 | |
| β-strand | 260-261 | 2 | 2 |
| β-strand | 264-268 | 5 | 2 |
| β-strand | 275-285 | 11 | 2 |
| β-strand | 290-300 | 11 | 2 |
| α-helix | 301-303 | 3 | |
| α-helix | 304-309 | 6 | |
| α-helix | 314-317 | 4 | |
| α-helix | 319-324 | 6 | |
| α-helix | 329-349 | 21 | |
| β-strand | 352-364 | 13 | 2 |
| β-strand | 372 | 1 | 2 |
| β-strand | 374-384 | 11 | 2 |
| β-strand | 417-419 | 3 | 2 |
| β-strand | 423-429 | 7 | 2 |
| α-helix | 437-438 | 2 | |
| α-helix | 439-446 | 8 | |
| β-strand | 451-452 | 2 | 2 |
| α-helix | 458-466 | 9 | |
| β-strand | 473-474 | 2 | 3 |
| α-helix | 478-480 | 3 | |
| α-helix | 606-608 | 3 | |
| β-strand | 612-613 | 2 | 3 |
| α-helix | 621-650 | 30 | |
| α-helix | 654-658 | 5 | |
| α-helix | 661-686 | 26 | |
| α-helix | 697-718 | 22 | |
Chain E: 14 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 206-211 | 6 | 4 |
| α-helix | 214-216 | 3 | |
| α-helix | 217-225 | 9 | |
| β-strand | 231-233 | 3 | 2 |
| α-helix | 235-237 | 3 | |
| β-strand | 296-302 | 7 | 4 |
| α-helix | 307-313 | 7 | |
| β-strand | 320-327 | 8 | 4 |
| α-helix | 330-332 | 3 | |
| β-strand | 336-343 | 8 | 4 |
| β-strand | 354-361 | 8 | 4 |
| α-helix | 366-370 | 5 | |
| α-helix | 376-385 | 10 | |
| α-helix | 392-412 | 21 | |
| β-strand | 415-428 | 14 | 4 |
| β-strand | 435-447 | 13 | 4 |
| β-strand | 481 | 1 | 5 |
| β-strand | 484 | 1 | 5 |
| β-strand | 486-487 | 2 | 4 |
| β-strand | 491-496 | 6 | 4 |
| α-helix | 509-515 | 7 | |
| β-strand | 520 | 1 | 4 |
| α-helix | 529-535 | 7 | |
| α-helix | 550-552 | 3 | |
| α-helix | 697-725 | 29 | |
| α-helix | 734-768 | 35 | |
| α-helix | 778-805 | 28 | |
Chain F: 4 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 761-795 | 35 | |
| α-helix | 806-834 | 29 | |
| α-helix | 840-842 | 3 | |
| α-helix | 843-868 | 26 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Vacuolar transporter chaperone complex subunit 1 | A | protein | 118 | Saccharomyces cerevisiae S288C | P40046 (AlphaFold model) |
| Vacuolar transporter chaperone complex subunit 1 | B, C | protein | 103 | Saccharomyces cerevisiae S288C | P40046 (AlphaFold model) |
| Vacuolar transporter chaperone complex subunit 4 | D | protein | 527 | Saccharomyces cerevisiae S288C | P47075 (AlphaFold model) |
| Vacuolar transporter chaperone 3 complex subunit 3 | E | protein | 604 | Saccharomyces cerevisiae S288C | Q02725 (AlphaFold model) |
| Vacuole transporter chaperone complex subunit 5 | F | protein | 110 | Saccharomyces cerevisiae S288C | P38966 (AlphaFold model) |
Sequence of entity 1 (A), FASTA
>9UMG_1 Vacuolar transporter chaperone complex subunit 1 (chains A)
PLLQRTPGKKIALPTRVEPKVFFANERTFLSWLNFTVMLGGLGVGLLNFGDKIGRVSAGL
FTFVAMGTMIYALVTYHWRAAAIRRRGSGPYDDRLGPTLLCFFLLVAVIINFILRLKY
Sequence of entity 2 (B, C), FASTA
>9UMG_2 Vacuolar transporter chaperone complex subunit 1 (chains B, C)
VEPKVFFANERTFLSWLNFTVMLGGLGVGLLNFGDKIGRVSAGLFTFVAMGTMIYALVTY
HWRAAAIRRRGSGPYDDRLGPTLLCFFLLVAVIINFILRLKYN
Sequence of entity 3 (D), FASTA
>9UMG_3 Vacuolar transporter chaperone complex subunit 4 (chains D)
RQTTKYWVHPDNITELKLIILKHLPVLVFNTNKEFEREDSAITSIYFDNENLDLYYGRLR
KDEGAEAHALAWYGGMSTDTIFVERKTHREDWTGEKSVKARFALKERHVNDFLKGKYTVD
QVFAKMRKEGKKPMNEIENLEALASEIQYVMLKKKLRPVVRSFYNRTAFQLPGDARVRIS
LDTELTMVREDNFDGVDRTHKNWRRTDIGVDWPFKQLDDKDICRFPYAVLNVKLQTQLGQ
EPPEWVRELVGSHLVEPVPKFSKFIHGVATLLNDKVDSIPFWLPQMDVDIRKPPLPTNIE
ITRPGRSDNEDNDFDEDDEDDAALVAAMTNAPGNSLDIEESVGYGATSAPTSNTNHVVES
ANAAYYQRKIRNAENPISKKYYEIVAFFDHYFNGDQISKIPKGTTFDTQIRAPPGKTICV
PVRVEPKVYFATERTYLSWLSISILLGGVSTTLLTYGSPTAMIGSIGFFITSLAVLIRTV
MVYAKRVVNIRLKRAVDYEDKIGPGMVSVFLILSILFSFFCNLVAKL
Sequence of entity 4 (E), FASTA
>9UMG_4 Vacuolar transporter chaperone 3 complex subunit 3 (chains E)
ASFKSYKFWVHDDNIMEVKARILRHLPALVYASVPNENDDFVDNLESDVRVQPEARLNIG
SKSNSLSSDGNSNQDVEIGKSKSVIFPQSYDPTITTLYFDNDFFDLYNNRLLKISGAPTL
RLRWIGKLLDKPDIFLEKRTFTENTETGNSSFEEIRLQMKAKFINNFIFKNDPSYKNYLI
NQLRERGTQKEELEKLSRDFDNIQNFIVEEKLQPVLRATYNRTAFQIPGDQSIRVTIDSN
IMYIREDSLDKNRPIRNPENWHRDDIDSNIPNPLRFLRAGEYSKFPYSVMEIKVINQDNS
QMPNYEWIKDLTNSHLVNEVPKFSLYLQGVASLFGEDDKYVNILPFWLPDLETDIRKNPQ
EAYEEEKKTLQKQKSIHDKLDNMRRLSKISVPDGKTTERQGQKDQNTRHVIADLEDHESS
DEEGTALPKKSAVKKGKKFKTNAAFLKILAGKNISENGNDPYSDDTDSASSFQLPPGVKK
PVHLLKNAGPVKVEAKVWLANERTFNRWLSVTTLLSVLTFSIYNSVQKAEFPQLADLLAY
VYFFLTLFCGVWAYRTYLKRLTLIKGRSGKHLDAPVGPILVAVVLIVTLVVNFSVAFKEA
ARRE
Sequence of entity 5 (F), FASTA
>9UMG_5 Vacuole transporter chaperone complex subunit 5 (chains F)
SIYEYRHDEVVTFLYLSALLTSCIMASVCLGIVLSLFRGQSNNEIDLEIQNILIAIIIIS
LLVSLILICACLLLLFSRFTLAPIWHYVGCFTMFFSVTGTVCYGMIEIFF
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| IHP | Inositol hexakisphosphate | C6 H18 O24 P6 | 3 |
Primary citation
Mechanistic insights into the regulation of polyphosphate polymerase VTC by the accessory subunit Vtc5. Zhang, J., Du, Z., Cheng, M. et al. Sci China Life Sci (2026) 69:1800-1803. DOI 10.1007/s11427-025-3127-8 · PubMed
Other PDB entries of the same protein (UniProt P40046 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 7YTJ 3.0 Å, Cryo-EM structure of VTC complex
- 8I6V 3.06 Å, Cryo-EM structure of the polyphosphate polymerase VTC complex(Vtc4/Vtc3/Vtc1)
Browse structure collections
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