1DK7: Isolated apical domain of groel

Crystal structure of an isolated apical domain of groel. Determined by X-ray diffraction at 2.02 Å resolution. Released 5 Jan 2000.

Method: X-ray diffraction
Resolution: 2.02 Å
Organism: Escherichia coli
Chains: 2
Atoms: 2,362
Mol. weight: 31.46 kDa
Released: 5 Jan 2000

Explore 1DK7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1DK7 contains 16 α-helices and 24 β-strands across 2 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: 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	256-267	12
β-strand	273-277	5	2
α-helix	278	1
α-helix	283-296	14
β-strand	300-301	2	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

Chain B: 9 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	193-195	3	4
β-strand	199	1	5
α-helix	202-204	3
β-strand	207	1	6
α-helix	208-210	3
β-strand	212	1	6
β-strand	213-216	4	4
β-strand	219-227	9	5
α-helix	231-233	3
α-helix	234-243	10
β-strand	247-254	8	5
α-helix	256-268	13
β-strand	273-277	5	5
α-helix	278	1
α-helix	282-296	15
β-strand	300-301	2	5
α-helix	309-311	3
α-helix	314-316	3
β-strand	318-319	2	5
β-strand	320-325	6	4
β-strand	330-335	6	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Groel	A, B	protein	146	Escherichia coli	P0A6F5 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1DK7_1 GROEL (chains A, B)
EGMQFDRGYLSPYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVAKAGKPLLII
AEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGMELE
KATLEDLGQAKRVVINKDTTTIIDGV

Primary citation

The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity. Chen, L., Sigler, P.B. Cell (1999) 99:757-768. DOI 10.1016/S0092-8674(00)81673-6 · 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
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
8BL2 2.3 Å, Structure of GroEL-ATP complex plunge frozen 200 ms after reaction initiation

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