1FY9: 60 kd chaperonin

Name: PDB 1FY9: Crystal structure of the hexa-substituted mutant of the molecular chaperonin groel apical domain
Published: 2000-11-22
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperone

Crystal structure of the hexa-substituted mutant of the molecular chaperonin groel apical domain. Determined by X-ray diffraction at 2.2 Å resolution. Released 22 Nov 2000.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Escherichia coli
Chains: 1
Atoms: 1,441
Mol. weight: 20.95 kDa
Released: 22 Nov 2000

Explore 1FY9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1FY9 contains 8 α-helices and 13 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: 8 helices, 13 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	219-223	5	3
β-strand	227	1	4
α-helix	230-243	14
β-strand	247-251	5	3
β-strand	254	1	4
α-helix	256-267	12
β-strand	273-277	5	3
α-helix	278	1
α-helix	282-296	15
β-strand	301	1	3
α-helix	309-311	3
β-strand	318-319	2	3
β-strand	320-325	6	1
β-strand	330-335	6	1
α-helix	339-354	16
α-helix	359-374	16

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
60 kd chaperonin	A	protein	193	Escherichia coli	P0A6F5 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1FY9_1 60 KD CHAPERONIN (chains A)
GLVPRGSEGMQFDRGYLSPYFINKPETGEVELESPFILLVDKKISNIRELLPVLEAVAKA
GKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISE
ELGMKLEKATLEDLGQAKRVVITKDTTTIIDGVGEEAAIQGRVAQIRQQIEEATSDYDRE
KLQERVAKLAGGV

Primary citation

Stabilization of GroEL minichaperones by core and surface mutations. Wang, Q., Buckle, A.M., Fersht, A.R. J Mol Biol (2000) 298:917-926. DOI 10.1006/jmbi.2000.3716 · 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
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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