3WVL: 60 kDa chaperonin

Crystal structure of the football-shaped GroEL-GroES complex (GroEL: GroES2:ATP14) from Escherichia coli. Determined by X-ray diffraction at 3.79 Å resolution. Released 17 Sept 2014.

Method: X-ray diffraction
Resolution: 3.79 Å
Organism: Escherichia coli
Chains: 28
Atoms: 64,540
Mol. weight: 955.85 kDa
Ligands: MG, ATP
Released: 17 Sept 2014

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

Secondary structure: helices and β-sheets

3WVL contains 300 α-helices and 445 β-strands across 28 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.

Chains a, O, Q, V, W, X, Y and Z: 1 helix, 9 β-strands

Element	Residues	Length	Sheet
β-strand	3-5	3	125
β-strand	9-14	6	9
β-strand	37-43	7	9
β-strand	46-47	2	10
β-strand	55-56	2	10
α-helix	57	1
β-strand	64-67	4	9
β-strand	74-78	5	9
β-strand	81-87	7	9
β-strand	91-95	5	9

Chain A: 22 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	1
α-helix	9-28	20
β-strand	37-40	4	2
β-strand	48-50	3	2
α-helix	53-59	7
α-helix	65-84	20
α-helix	89-108	20
α-helix	113-134	22
β-strand	136	1	3
α-helix	141-151	11
α-helix	156-169	14
β-strand	175-179	5	4
β-strand	186-191	6	4
β-strand	193-195	3	5
β-strand	199	1	6
β-strand	213-216	4	5
β-strand	219-222	4	6
α-helix	231-233	3
α-helix	234-241	8
β-strand	247-251	5	6
α-helix	256-268	13
β-strand	273-277	5	6
α-helix	283-296	14
β-strand	318-319	2	6
β-strand	320	1	7
β-strand	322-325	4	5
β-strand	330-332	3	5
β-strand	335	1	7
α-helix	339-349	11
α-helix	350-355	6
α-helix	358-369	12
β-strand	375-381	7	4
α-helix	386-409	24
β-strand	411-413	3	3
α-helix	417-425	9
α-helix	426-428	3
α-helix	434-446	13
α-helix	449-457	9
α-helix	462-470	9
β-strand	476-479	4	8
β-strand	484-487	4	8
α-helix	488-491	4
β-strand	494-496	3	3
α-helix	497-514	18
β-strand	517-523	7	1

Chain b: 1 helix, 9 β-strands

Element	Residues	Length	Sheet
β-strand	3-5	3	9
β-strand	9-14	6	17
β-strand	37-43	7	17
β-strand	47	1	18
β-strand	55	1	18
α-helix	56-57	2
β-strand	64-67	4	17
β-strand	74-78	5	17
β-strand	81-87	7	17
β-strand	91-95	5	17

Chain B: 21 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	11
α-helix	9-28	20
β-strand	37-40	4	1
β-strand	48-50	3	1
α-helix	53-59	7
α-helix	65-84	20
α-helix	89-108	20
α-helix	113-134	22
β-strand	136	1	12
α-helix	141-151	11
α-helix	156-169	14
β-strand	175-179	5	13
β-strand	186-190	5	13
β-strand	193-195	3	14
β-strand	199	1	15
β-strand	213-216	4	14
β-strand	219-222	4	15
α-helix	231-233	3
α-helix	234-243	10
β-strand	247-251	5	15
α-helix	256-268	13
β-strand	273-277	5	15
α-helix	283-296	14
β-strand	318-319	2	15
β-strand	320-325	6	14
β-strand	330-335	6	14
α-helix	339-353	15
α-helix	360-370	11
β-strand	376-381	6	13
α-helix	386-409	24
β-strand	411-413	3	12
α-helix	417-425	9
α-helix	426-428	3
α-helix	434-446	13
α-helix	449-457	9
α-helix	462-470	9
β-strand	476-479	4	16
β-strand	484-487	4	16
α-helix	488-491	4
β-strand	494-496	3	12
α-helix	497-514	18
β-strand	517-523	7	11

Chain C: 20 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	19
α-helix	9-28	20
β-strand	37-40	4	11
β-strand	48-50	3	11
α-helix	53-59	7
α-helix	65-84	20
α-helix	89-108	20
α-helix	113-134	22
β-strand	136	1	20
α-helix	141-151	11
α-helix	156-169	14
β-strand	174-179	6	21
β-strand	186-190	5	21
β-strand	194-195	2	22
β-strand	199	1	23
β-strand	213-216	4	22
β-strand	219-222	4	23
α-helix	231-233	3
α-helix	234-243	10
β-strand	247-251	5	23
α-helix	256-268	13
β-strand	273-277	5	23
α-helix	283-296	14
β-strand	318-319	2	23
β-strand	320	1	24
β-strand	322-325	4	22
β-strand	330-332	3	22
β-strand	335	1	24
α-helix	339-353	15
α-helix	360-370	11
β-strand	376-381	6	21
α-helix	386-409	24
β-strand	411-413	3	20
α-helix	417-425	9
α-helix	426-428	3
α-helix	434-446	13
α-helix	449-458	10
α-helix	462-471	10
β-strand	476-479	4	25
β-strand	484-487	4	25
β-strand	494-496	3	20
α-helix	497-514	18
β-strand	517-523	7	19

Chain D: 19 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	26
α-helix	9-28	20
β-strand	37-40	4	19
β-strand	48-50	3	19
α-helix	53-59	7
α-helix	65-84	20
α-helix	89-108	20
α-helix	113-134	22
β-strand	136	1	27
α-helix	141-151	11
α-helix	156-169	14
β-strand	175-179	5	28
β-strand	186-190	5	28
β-strand	194-195	2	29
β-strand	199	1	30
β-strand	213-216	4	29
β-strand	219-222	4	30
α-helix	231-233	3
α-helix	234-243	10
β-strand	247-251	5	30
α-helix	256-267	12
β-strand	273-277	5	30
α-helix	283-296	14
β-strand	318-319	2	30
β-strand	320	1	31
β-strand	322-325	4	29
β-strand	330-332	3	29
β-strand	335	1	31
α-helix	339-353	15
α-helix	360-370	11
β-strand	376-381	6	28
α-helix	386-409	24
β-strand	411-413	3	27
α-helix	417-425	9
α-helix	434-446	13
α-helix	449-458	10
α-helix	462-471	10
β-strand	476-479	4	32
β-strand	484-487	4	32
β-strand	494-496	3	27
α-helix	497-514	18
β-strand	517-523	7	26

Chain E: 21 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	33
α-helix	9-28	20
β-strand	37-40	4	26
β-strand	48-50	3	26
α-helix	53-59	7
α-helix	65-84	20
α-helix	89-108	20
α-helix	113-134	22
β-strand	136	1	34
α-helix	141-151	11
α-helix	156-169	14
β-strand	175-179	5	35
β-strand	186-190	5	35
β-strand	194-195	2	36
β-strand	199	1	37
β-strand	213-216	4	36
β-strand	219-222	4	37
α-helix	231-233	3
α-helix	234-243	10
β-strand	247-251	5	37
α-helix	256-268	13
β-strand	273-277	5	37
α-helix	283-296	14
β-strand	318-319	2	37
β-strand	320	1	38
β-strand	322-325	4	36
β-strand	330-332	3	36
β-strand	335	1	38
α-helix	339-353	15
α-helix	361-370	10
β-strand	376-381	6	35
α-helix	386-409	24
β-strand	411-413	3	34
α-helix	417-425	9
α-helix	426-428	3
α-helix	434-446	13
α-helix	449-457	9
α-helix	462-471	10
β-strand	476-479	4	39
β-strand	484-487	4	39
α-helix	488-491	4
β-strand	494-496	3	34
α-helix	497-514	18
β-strand	517-523	7	33

Chain F: 20 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	40
α-helix	9-28	20
β-strand	37-40	4	33
β-strand	48-50	3	33
α-helix	53-59	7
α-helix	65-84	20
α-helix	89-108	20
α-helix	113-134	22
β-strand	136	1	41
α-helix	141-151	11
α-helix	156-169	14
β-strand	174-179	6	42
β-strand	186-190	5	42
β-strand	193-195	3	43
β-strand	213-216	4	43
β-strand	219-222	4	44
α-helix	231-233	3
α-helix	234-243	10
β-strand	247-251	5	44
α-helix	256-268	13
β-strand	273-277	5	44
α-helix	283-296	14
β-strand	318-319	2	44
β-strand	320	1	45
β-strand	322-325	4	43
β-strand	330-332	3	43
β-strand	335	1	45
α-helix	339-353	15
α-helix	360-370	11
β-strand	376-381	6	42
α-helix	386-409	24
β-strand	411-413	3	41
α-helix	417-425	9
α-helix	426-428	3
α-helix	434-446	13
α-helix	449-457	9
α-helix	462-471	10
β-strand	476-479	4	46
β-strand	484-487	4	46
β-strand	494-496	3	41
α-helix	497-514	18
β-strand	517-523	7	40

13 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
60 kDa chaperonin	A, B, C, D, E, F, G, H, I, J, K, L, M, N	protein	548	Escherichia coli	P0A6F5 (AlphaFold model)
10 kDa chaperonin	O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b	protein	97	Escherichia coli	P0A6F9 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K, L, M, N), FASTA

>3WVL_1 60 kDa chaperonin (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N)
MAAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKAGVSVAREI
ELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIITEGLKAVAAGMNPMDLKRGI
DKAVTAAVEELKALSVPCSDSKAIAQVGTISANSDETVGKLIAEAMDKVGKEGVITVEDG
TGLQDELDVVEGMQFDRGYLSPYFINKPETGAVELESPFILLADKKISNIREMLPVLEAV
AKAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTV
ISEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQQIEEATSDY
DREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEAALHATRAAVEEGVVAGGGVALI
RVASKLADLRGQNEDQNVGIKVALRAMEAPLRQIVLNCGEEPSVVANTVKGGDGNYGYNA
ATEEYGNMIDMGILDPTKVTRSALQYAASVAGLMITTECMVTDLPKNDAADLGAAGGMGG
MGGMGGMM

Sequence of entity 2 (O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b), FASTA

>3WVL_2 10 kDa chaperonin (chains O, P, Q, R, S, T, U, V, W, X, Y, Z, a, b)
MNIRPLHDRVIVKRKEVETKSAGGIVLTGSAAAKSTRGEVLAVGNGRILENGEVKPLDVK
VGDIVIFNDGYGVKSEKIDNEEVLIMSESDILAIVEA

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	14
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	14

Water and common crystallization additives (K) are not listed.

Primary citation

Crystal structure of a symmetric football-shaped GroEL:GroES2-ATP14 complex determined at 3.8 angstrom reveals rearrangement between two GroEL rings. Koike-Takeshita, A., Arakawa, T., Taguchi, H. et al. J Mol Biol (2014) 426:3634-3641. DOI 10.1016/j.jmb.2014.08.017 · 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
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

Browse structure collections

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