1KID: Groel

Groel (HSP60 class) fragment (apical domain) comprising residues 191-376, mutant with ala 262 replaced with leu and ile 267 replaced with met. Determined by X-ray diffraction at 1.7 Å resolution. Released 17 Sept 1997.

Method: X-ray diffraction
Resolution: 1.7 Å
Organism: Escherichia coli
Chains: 1
Atoms: 1,746
Mol. weight: 22.06 kDa
Released: 17 Sept 1997

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

Secondary structure: helices and β-sheets

1KID contains 10 α-helices and 14 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, 14 β-strands

Element	Residues	Length	Sheet
β-strand	193-195	3	1
α-helix	202-204	3
β-strand	207	1	2
β-strand	212	1	2
β-strand	213-216	4	1
β-strand	219-222	4	3
β-strand	223	1	4
β-strand	226-227	2	5
α-helix	230-243	14
β-strand	247-251	5	3
β-strand	253-254	2	5
α-helix	256-267	12
β-strand	273-277	5	3
α-helix	278-279	2
α-helix	282-296	15
β-strand	301	1	4
α-helix	303-305	3
α-helix	309-311	3
α-helix	314-316	3
β-strand	318-319	2	3
β-strand	320-325	6	1
β-strand	330-335	6	1
α-helix	339-355	17
α-helix	359-375	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Groel (HSP60 class)	A	protein	203	Escherichia coli	P0A6F5 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1KID_1 GROEL (HSP60 CLASS) (chains A)
MRGSHHHHHHGLVPRGSEGMQFDRGYLSPYFINKPETGAVELESPFILLADKKISNIREM
LPVLEAVAKAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIA
TLTGGTVISEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQQI
EEATSDYDREKLQERVAKLAGGV

Primary citation

A structural model for GroEL-polypeptide recognition. Buckle, A.M., Zahn, R., Fersht, A.R. Proc Natl Acad Sci U S A (1997) 94:3571-3575. DOI 10.1073/pnas.94.8.3571 · 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…
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
8BL2 2.3 Å, Structure of GroEL-ATP complex plunge frozen 200 ms after reaction initiation

Browse structure collections

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