1LA1: GroEL

Gro-EL Fragment (Apical Domain) Comprising Residues 188-379. Determined by X-ray diffraction at 2.06 Å resolution. Released 3 Apr 2002.

Method: X-ray diffraction
Resolution: 2.06 Å
Organism: Escherichia coli
Chains: 1
Atoms: 1,722
Mol. weight: 20.73 kDa
Released: 3 Apr 2002

Explore 1LA1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1LA1 contains 10 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: 10 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	301	1	2
α-helix	303-305	3
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
α-helix	339-354	16
α-helix	359-375	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
GroEL	A	protein	192	Escherichia coli	P0A6F5 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1LA1_1 GroEL (chains A)
DVVEGMQFDRGYLSPYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVAKAGKPL
LIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGM
ELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQQIEEATSDYDREKLQE
RVAKLAGGVAVI

Primary citation

Structural plasticity and noncovalent substrate binding in the GroEL apical domain. A study using electrospay ionization mass spectrometry and fluorescence binding studies. Ashcroft, A.E., Brinker, A., Coyle, J.E. et al. J Biol Chem (2002) 277:33115-33126. DOI 10.1074/jbc.M203398200 · 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
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
8BL2 2.3 Å, Structure of GroEL-ATP complex plunge frozen 200 ms after reaction initiation

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