1JON: Groel, HSP60 class

Name: PDB 1JON: Groel (HSP60 class) fragment comprising residues 191-345
Published: 1997-03-12
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperone

Groel (HSP60 class) fragment comprising residues 191-345. Determined by X-ray diffraction at 2.5 Å resolution. Released 12 Mar 1997.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Escherichia coli
Chains: 1
Atoms: 1,033
Mol. weight: 16.64 kDa
Released: 12 Mar 1997

Explore 1JON in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1JON contains 7 α-helices and 12 β-strands across 1 chain. 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: 7 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	193-195	3	1
β-strand	199	1	2
α-helix	202-204	3
β-strand	207	1	3
β-strand	212	1	3
β-strand	213-216	4	1
β-strand	219-227	9	2
α-helix	230-243	14
β-strand	247-254	8	2
α-helix	256-268	13
β-strand	273-277	5	2
α-helix	278	1
α-helix	282-296	15
β-strand	300	1	2
α-helix	309-311	3
α-helix	314-316	3
β-strand	318-319	2	2
β-strand	320-325	6	1
β-strand	330-335	6	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Groel, HSP60 class	A	protein	155	Escherichia coli	P0A6F5 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1JON_1 GROEL, HSP60 CLASS (chains A)
EGMQFDRGYLSPYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVAKAGKPLLII
AEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGMELE
KATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGR

Primary citation

Chaperone activity and structure of monomeric polypeptide binding domains of GroEL. Zahn, R., Buckle, A.M., Perrett, S. et al. Proc Natl Acad Sci U S A (1996) 93:15024-15029. DOI 10.1073/pnas.93.26.15024 · PubMed

Other PDB entries of the same protein (UniProt P0A6F5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3VZ6 1.5 Å, Crystal Structure Analysis of the Mini-chaperonines, variant with Gly 184 replaced with…
1KID 1.7 Å, Groel (HSP60 class) fragment (apical domain) comprising residues 191-376, mutant with…
3VZ7 1.8 Å, Crystal Structure Analysis of the mini-chaperonin variant with Pro 187 Gly
3VZ8 1.9 Å, Crystal Structure Analysis of the Mini-chaperonin variant with Leu 185, Val 186, Pro…
1KP8 2.0 Å, Structural Basis for GroEL-assisted Protein Folding from the Crystal Structure of…
1SX3 2.0 Å, GroEL14-(ATPgammaS)14
1DK7 2.02 Å, Crystal structure of an isolated apical domain of groel
1LA1 2.06 Å, Gro-EL Fragment (Apical Domain) Comprising Residues 188-379
1DKD 2.1 Å, Crystal structure of a groel (apical domain) and a dodecameric peptide complex
1FY9 2.2 Å, Crystal structure of the hexa-substituted mutant of the molecular chaperonin groel…
1FYA 2.2 Å, Crystal structure of the hexa-substituted mutant of the molecular chaperonin groel…
8BKZ 2.3 Å, GroEL:GroES-ATP complex under continuous turnover conditions

Browse structure collections

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