3VZ6: 60 kDa chaperonin

Name: PDB 3VZ6: Crystal Structure Analysis of the Mini-chaperonines, variant with Gly 184 replaced with Ile and Leu 185 replaced Val and Val 186 replaced with Leu.
Published: 2013-11-13
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperone

Crystal Structure Analysis of the Mini-chaperonines, variant with Gly 184 replaced with Ile and Leu 185 replaced Val and Val 186 replaced with Leu. Determined by X-ray diffraction at 1.5 Å resolution. Released 13 Nov 2013.

Method: X-ray diffraction
Resolution: 1.5 Å
Organism: Escherichia coli
Chains: 1
Atoms: 1,577
Mol. weight: 21.6 kDa
Released: 13 Nov 2013

Explore 3VZ6 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3VZ6 contains 11 α-helices and 15 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: 11 helices, 15 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	219-222	4	2
β-strand	223	1	4
β-strand	226-227	2	5
α-helix	230-233	4
α-helix	234-243	10
β-strand	247-251	5	2
β-strand	253-254	2	5
α-helix	256-267	12
β-strand	273-277	5	2
α-helix	278	1
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	2
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
60 kDa chaperonin	A	protein	199	Escherichia coli	P0A6F5 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3VZ6_1 60 kDa chaperonin (chains A)
HHHHHHIVLTGSAEGMQFDRGYLSPYFINKPETGAVELESPFILLADKKISNIREMLPVL
EAVAKAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTG
GTVISEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQQIEEAT
SDYDREKLQERVAKLAGGV

Primary citation

Binding Energy(BE) from Crystal Packing of Mini-chaperones (mcpn) Provided Insights into the Allosteric Interaction of GroEL/ES Complex. Saijo, S., Sato, T. To be published.

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

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
8BL2 2.3 Å, Structure of GroEL-ATP complex plunge frozen 200 ms after reaction initiation

Browse structure collections

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