Structure of GroEL-ATP complex plunge frozen 200 ms after reaction initiation. Determined by electron microscopy at 2.3 Å resolution. Released 9 Aug 2023.
Explore 8BL2 in 3D Show helices and sheets RCSB PDB PDBe
8BL2 contains 364 α-helices and 336 β-strands across 14 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-8 | 5 | 2 |
| α-helix | 9-28 | 20 | |
| β-strand | 37-40 | 4 | 9 |
| α-helix | 41 | 1 | |
| α-helix | 47 | 1 | |
| β-strand | 48-50 | 3 | 9 |
| α-helix | 53-59 | 7 | |
| α-helix | 65-85 | 21 | |
| α-helix | 89-108 | 20 | |
| α-helix | 113-134 | 22 | |
| α-helix | 135 | 1 | |
| β-strand | 136 | 1 | 10 |
| α-helix | 137 | 1 | |
| α-helix | 138-141 | 4 | |
| α-helix | 144-151 | 8 | |
| α-helix | 156-169 | 14 | |
| β-strand | 174-179 | 6 | 11 |
| β-strand | 186-190 | 5 | 11 |
| β-strand | 193-195 | 3 | 12 |
| β-strand | 199 | 1 | 13 |
| α-helix | 202-204 | 3 | |
| β-strand | 213-216 | 4 | 12 |
| β-strand | 219-223 | 5 | 13 |
| α-helix | 226-227 | 2 | |
| α-helix | 234-240 | 7 | |
| β-strand | 247-251 | 5 | 13 |
| α-helix | 260-266 | 7 | |
| β-strand | 273-277 | 5 | 13 |
| α-helix | 283-296 | 14 | |
| β-strand | 300-301 | 2 | 13 |
| α-helix | 309-311 | 3 | |
| β-strand | 318-319 | 2 | 13 |
| β-strand | 320 | 1 | 14 |
| β-strand | 322-325 | 4 | 12 |
| β-strand | 330-332 | 3 | 12 |
| β-strand | 335 | 1 | 14 |
| α-helix | 339-355 | 17 | |
| α-helix | 359-374 | 16 | |
| β-strand | 376-381 | 6 | 11 |
| α-helix | 386-409 | 24 | |
| β-strand | 411-413 | 3 | 10 |
| α-helix | 417-425 | 9 | |
| α-helix | 434-446 | 13 | |
| α-helix | 449-457 | 9 | |
| α-helix | 462-471 | 10 | |
| β-strand | 476-479 | 4 | 15 |
| β-strand | 484-487 | 4 | 15 |
| β-strand | 494-496 | 3 | 10 |
| α-helix | 497-514 | 18 | |
| β-strand | 517-523 | 7 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Chaperonin GroEL | A, B, C, D, E, F, G, H, I, J, K, L, M, N | protein | 548 | Escherichia coli | P0A6F5 (AlphaFold model) |
>8BL2_1 Chaperonin GroEL (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N) MAAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREI ELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIITEGLKAVAAGMNPMDLKRGI DKAVTAAVEELKALSVPCSDSKAIAQVGTISANSDETVGKLIAEAMDKVGKEGVITVEDG TGLQDELDVVEGMQFDRGYLSPYFINKPETGAVELESPFILLADKKISNIREMLPVLEAV AKAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTV ISEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQQIEEATSDY DREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGVVAGGGVALI RVASKLADLRGQNEDQNVGIKVALRAMEAPLRQIVLNCGEEPSVVANTVKGGDGNYGYNA ATEEYGNMIDMGILDPTKVTRSALQYAASVAGLMITTECMVTDLPKNDAADLGAAGGMGG MGGMGGMM
Water and common crystallization additives (K) are not listed.
Time-resolved cryo-EM using a combination of droplet microfluidics with on-demand jetting. Torino, S., Dhurandhar, M., Stroobants, A. et al. Nat Methods (2023) 20:1400-1408. DOI 10.1038/s41592-023-01967-z · PubMed
Other PDB entries of the same protein (UniProt P0A6F5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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