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3IYF: 
Atomic Model of the Lidless Mm-cpn in the Open State
Biological unit 1: hexadecameric
Source organism: Methanococcus maripaludis
Number of proteins:
16 (Chaperonin ▼)
Protein molecule
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GG -Click to explore this molecule neighborsHH -Click to explore this molecule neighborsII -Click to explore this molecule neighborsJJ -Click to explore this molecule neighborsKK -Click to explore this molecule neighbors
LL -Click to explore this molecule neighborsMM -Click to explore this molecule neighborsNN -Click to explore this molecule neighborsOO -Click to explore this molecule neighborsPP -Click to explore this molecule neighbors
 Chaperonin
Similar Structures (131)help
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Showing 1 to 10 out of 131 selected structures help
      PDB ID Description Taxonomy▲▼ Aligned Protein▲▼ RMSD▲▼ Aligned Residues▲▼ Sequence Identity▲▼
1
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 3J02
Lidless D386A Mm-cpn in the pre-hydrolysis ATP-bound state
Methanococcus maripaludis
 16 4.22Å 7856 99%
2
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 3KFK
Crystal structures of a group II chaperonin from Methanococcus maripaludis
Methanococcus maripaludis
 16 5.25Å 7756 97%
3
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 3J1C
Cryo-EM structure of 9-fold symmetric rATcpn-alpha in apo state
Acidianus tengchongensis
 16 16.18Å 7731 49%
4
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 3J1B
Cryo-EM structure of 8-fold symmetric rATcpn-alpha in apo state
Acidianus tengchongensis
 16 8.67Å 7724 48%
5
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 3J1E
Cryo-EM structure of 9-fold symmetric rATcpn-beta in apo state
Acidianus tengchongensis
 16 11.63Å 7664 49%
6
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 6NR8
hTRiC-hPFD Class6
Homo sapiens
 16 9.27Å 7610 35%
7
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 6NRA
hTRiC-hPFD Class1 (No PFD)
Homo sapiens
 16 9.58Å 7595 34%
8
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 6QB8
Human CCT:mLST8 complex
Homo sapiens
 16 9.68Å 7561 36%
9
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 6NRD
hTRiC-hPFD Class4
Homo sapiens
 16 9.58Å 7558 33%
10
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 4A0V
model refined against the Symmetry-free cryo-EM map of TRiC-AMP-PNP
Bos taurus
 16 8.78Å 7548 30%
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{"1":"Chaperonin","2":"Chaperonin","3":"Chaperonin","4":"Chaperonin","5":"Chaperonin","6":"Chaperonin","7":"Chaperonin","8":"Chaperonin","9":"Chaperonin","10":"Chaperonin","11":"Chaperonin","12":"Chaperonin","13":"Chaperonin","14":"Chaperonin","15":"Chaperonin","16":"Chaperonin"}
Citing VAST
Gibrat JF, Madej T, Bryant SH. "Surprising similarities in structure comparison.", Curr Opin Struct Biol.1996 Jun;6(3):377-85
Madej T, Lanczycki CJ, Zhang D, Thiessen PA, Geer RC, Marchler-Bauer A, Bryant SH. "MMDB and VAST+: tracking structural similarities between macromolecular complexes." Nucl. Acids Res. 2014 Jan;42(Database issue):D297-303
Thomas Madej, Aron Marchler-Bauer, Christopher Lanczycki, Dachuan Zhang, Stephen H Bryant "Biological Assembly Comparison With VAST" Methods Mol. Biol. 2020(2112):175-186
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?Original VAST
Original VAST finds structures that are similar to individual protein molecules, or individual 3D domains, in your query structure. Select a protein molecule ("chain") or 3D domain of interest from the table below to view a list of other proteins or domains that have a similar 3D shape. In contrast to VAST+, which focuses on the default biological unit, Original VAST lists all protein molecules in the asymmetric unit of the query structure.