7XOK: Chaperonin GroEL

Cryo-EM structure of double occupied ring (DOR) of GroEL-UGT1A complex at 2.7 Ang. resolution. Determined by electron microscopy at 2.7 Å resolution. Released 3 May 2023.

Method: Electron microscopy
Resolution: 2.7 Å
Organism: Escherichia coli
Chains: 14
Atoms: 53,970
Mol. weight: 801.65 kDa
Released: 3 May 2023

Explore 7XOK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7XOK contains 287 α-helices and 369 β-strands across 14 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 and J: 19 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	1
α-helix	10-28	19
β-strand	37-40	4	2
β-strand	48-50	3	2
α-helix	53-59	7
α-helix	65-85	21
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	174-179	6	4
β-strand	186-190	5	4
β-strand	193-195	3	5
β-strand	199	1	6
α-helix	202-204	3
β-strand	207	1	7
β-strand	212	1	7
β-strand	213-216	4	5
β-strand	219-223	5	6
β-strand	227	1	8
α-helix	230-243	14
β-strand	247-251	5	6
β-strand	254	1	8
α-helix	257-268	12
β-strand	273-277	5	6
α-helix	278	1
α-helix	283-296	14
β-strand	300-301	2	6
β-strand	318-319	2	6
β-strand	320-325	6	5
β-strand	330-335	6	5
α-helix	339-355	17
α-helix	359-373	15
β-strand	376-381	6	4
α-helix	386-409	24
β-strand	411-413	3	3
α-helix	417-426	10
α-helix	434-457	24
α-helix	462-471	10
β-strand	476-479	4	9
β-strand	484-487	4	9
β-strand	494-496	3	3
α-helix	497-515	19
β-strand	517-523	7	1

Chain B: 21 helices, 28 β-strands

Element	Residues	Length	Sheet
β-strand	4-5	2	10
β-strand	8	1	2
α-helix	10-28	19
β-strand	37-40	4	11
α-helix	47	1
β-strand	48-50	3	11
α-helix	53-59	7
α-helix	65-85	21
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	174-179	6	13
β-strand	186-190	5	13
β-strand	193-195	3	14
β-strand	199	1	15
α-helix	202-204	3
β-strand	207	1	16
β-strand	212	1	16
β-strand	213-216	4	14
β-strand	219-223	5	15
β-strand	227	1	17
α-helix	230-243	14
β-strand	247-251	5	15
β-strand	254	1	17
α-helix	257-268	12
β-strand	273-277	5	15
α-helix	278	1
α-helix	283-296	14
β-strand	300-301	2	15
β-strand	318-319	2	15
β-strand	320-325	6	14
β-strand	330-335	6	14
α-helix	339-355	17
α-helix	359-373	15
β-strand	376-381	6	13
α-helix	386-409	24
β-strand	411-413	3	12
α-helix	417-426	10
α-helix	434-457	24
α-helix	462-471	10
β-strand	476-479	4	18
β-strand	484-487	4	18
α-helix	488-491	4
β-strand	494-496	3	12
α-helix	497-515	19
β-strand	517-521	5	2
β-strand	522-523	2	10

Chain C: 22 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	11
α-helix	10-28	19
β-strand	37-40	4	19
β-strand	48-50	3	19
α-helix	53-59	7
α-helix	65-85	21
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	192-195	4	22
β-strand	199	1	23
α-helix	202-204	3
β-strand	207	1	24
β-strand	212	1	24
β-strand	213-216	4	22
β-strand	219-223	5	23
β-strand	227	1	25
α-helix	230-232	3
α-helix	234-243	10
β-strand	247-251	5	23
β-strand	254	1	25
α-helix	257-268	12
β-strand	273-277	5	23
α-helix	278	1
α-helix	283-296	14
β-strand	300-301	2	23
α-helix	309-311	3
β-strand	318-319	2	23
β-strand	320-325	6	22
β-strand	330-335	6	22
α-helix	339-355	17
α-helix	359-373	15
β-strand	376-381	6	21
α-helix	386-409	24
β-strand	411-413	3	20
α-helix	417-425	9
α-helix	434-457	24
α-helix	462-471	10
β-strand	476-479	4	26
β-strand	484-487	4	26
α-helix	488-491	4
β-strand	494-496	3	20
α-helix	497-515	19
β-strand	517-523	7	11

Chains D and E: 20 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	19
α-helix	10-28	19
β-strand	37-40	4	27
α-helix	47	1
β-strand	48-50	3	27
α-helix	53-59	7
α-helix	65-85	21
α-helix	89-108	20
α-helix	113-134	22
β-strand	136	1	28
α-helix	141-151	11
α-helix	156-169	14
β-strand	174-179	6	29
β-strand	186-190	5	29
β-strand	193-195	3	30
β-strand	199	1	31
α-helix	202-204	3
β-strand	207	1	30
β-strand	212-216	5	30
β-strand	219-222	4	31
β-strand	223	1	32
β-strand	227	1	33
α-helix	230-243	14
β-strand	247-251	5	31
β-strand	254	1	33
α-helix	257-268	12
β-strand	273-277	5	31
α-helix	278	1
α-helix	283-296	14
β-strand	301	1	32
β-strand	318-319	2	31
β-strand	320-326	7	30
β-strand	330-335	6	30
α-helix	339-355	17
α-helix	359-373	15
β-strand	376-381	6	29
α-helix	386-409	24
β-strand	411-413	3	28
α-helix	417-426	10
α-helix	434-457	24
α-helix	462-471	10
β-strand	476-479	4	34
β-strand	484-487	4	34
β-strand	494-496	3	28
α-helix	497-515	19
β-strand	517-523	7	19

Chain F: 22 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	35
α-helix	10-28	19
β-strand	37-40	4	43
α-helix	47	1
β-strand	48-50	3	43
α-helix	53-59	7
α-helix	65-85	21
α-helix	89-108	20
α-helix	113-134	22
β-strand	136	1	44
α-helix	141-151	11
α-helix	156-169	14
β-strand	174-179	6	45
β-strand	186-190	5	45
β-strand	193-195	3	46
β-strand	199	1	47
α-helix	202-204	3
β-strand	207	1	48
β-strand	212	1	48
β-strand	213-216	4	46
β-strand	219-222	4	47
β-strand	223	1	49
β-strand	227	1	50
α-helix	230-232	3
α-helix	234-243	10
β-strand	247-251	5	47
β-strand	254	1	50
α-helix	257-268	12
β-strand	273-277	5	47
α-helix	278	1
α-helix	283-296	14
β-strand	301	1	49
β-strand	318-319	2	47
β-strand	320-325	6	46
β-strand	330-335	6	46
α-helix	339-355	17
α-helix	359-373	15
β-strand	376-381	6	45
α-helix	386-409	24
β-strand	411-413	3	44
α-helix	417-426	10
α-helix	434-457	24
α-helix	462-471	10
β-strand	476-479	4	51
β-strand	484-487	4	51
α-helix	488-491	4
β-strand	494-496	3	44
α-helix	497-515	19
β-strand	517-523	7	35

Chain G: 21 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	43
α-helix	10-28	19
β-strand	37-40	4	1
β-strand	48-50	3	1
α-helix	53-58	6
α-helix	65-85	21
α-helix	89-108	20
α-helix	113-134	22
β-strand	136	1	52
α-helix	141-151	11
α-helix	156-169	14
β-strand	174-179	6	53
β-strand	186-190	5	53
β-strand	193-195	3	54
β-strand	199	1	55
α-helix	202-204	3
β-strand	207	1	54
β-strand	212-216	5	54
β-strand	219-222	4	55
β-strand	223	1	56
β-strand	227	1	57
α-helix	230-232	3
α-helix	234-243	10
β-strand	247-251	5	55
β-strand	254	1	57
α-helix	257-268	12
β-strand	273-277	5	55
α-helix	278	1
α-helix	283-296	14
β-strand	301	1	56
β-strand	318-319	2	55
β-strand	320-326	7	54
β-strand	330-335	6	54
α-helix	339-355	17
α-helix	359-374	16
β-strand	376-381	6	53
α-helix	386-409	24
β-strand	411-413	3	52
α-helix	417-426	10
α-helix	434-457	24
α-helix	462-471	10
β-strand	476-479	4	58
β-strand	484-487	4	58
α-helix	488-491	4
β-strand	494-496	3	52
α-helix	497-515	19
β-strand	517-523	7	43

Chain H: 20 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	59
α-helix	10-28	19
β-strand	37-40	4	60
β-strand	48-50	3	60
α-helix	53-59	7
α-helix	65-85	21
α-helix	89-108	20
α-helix	113-134	22
β-strand	136	1	61
α-helix	141-151	11
α-helix	156-169	14
β-strand	174-179	6	62
β-strand	186-190	5	62
β-strand	193-195	3	63
β-strand	199	1	64
α-helix	202-204	3
β-strand	207	1	65
β-strand	212	1	65
β-strand	213-216	4	63
β-strand	219-223	5	64
β-strand	227	1	66
α-helix	230-243	14
β-strand	247-251	5	64
β-strand	254	1	66
α-helix	257-268	12
β-strand	273-277	5	64
α-helix	278	1
α-helix	283-296	14
β-strand	300-301	2	64
β-strand	318-319	2	64
β-strand	320-325	6	63
β-strand	330-335	6	63
α-helix	339-355	17
α-helix	359-374	16
β-strand	376-381	6	62
α-helix	386-409	24
β-strand	411-413	3	61
α-helix	417-426	10
α-helix	434-457	24
α-helix	462-471	10
β-strand	476-479	4	67
β-strand	484-487	4	67
α-helix	488-491	4
β-strand	494-496	3	61
α-helix	497-515	19
β-strand	517-523	7	59

Chain I: 20 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	60
α-helix	10-28	19
β-strand	37-40	4	68
α-helix	47	1
β-strand	48-50	3	68
α-helix	53-59	7
α-helix	65-85	21
α-helix	89-109	21
α-helix	113-134	22
β-strand	136	1	69
α-helix	141-151	11
α-helix	156-169	14
β-strand	174-179	6	70
β-strand	186-190	5	70
β-strand	192-195	4	71
β-strand	199	1	72
α-helix	202-204	3
β-strand	207	1	73
β-strand	212	1	73
β-strand	213-216	4	71
β-strand	219-223	5	72
β-strand	227	1	74
α-helix	230-243	14
β-strand	247-251	5	72
β-strand	254	1	74
α-helix	256-268	13
β-strand	273-277	5	72
α-helix	278	1
α-helix	283-296	14
β-strand	300-301	2	72
β-strand	318-319	2	72
β-strand	320-325	6	71
β-strand	330-335	6	71
α-helix	339-355	17
α-helix	359-374	16
β-strand	376-381	6	70
α-helix	386-409	24
β-strand	411-413	3	69
α-helix	417-425	9
α-helix	434-457	24
α-helix	462-471	10
β-strand	476-478	3	75
β-strand	485-487	3	75
β-strand	494-496	3	69
α-helix	497-515	19
β-strand	517-523	7	60

4 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
Chaperonin GroEL	A, B, C, D, E, F, G, H, I, J, K, L, M, N	protein	547	Escherichia coli	P0A6F5 (AlphaFold model)

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

>7XOK_1 Chaperonin GroEL (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N)
AAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIE
LEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIITEGLKAVAAGMNPMDLKRGID
KAVTAAVEELKALSVPCSDSKAIAQVGTISANSDETVGKLIAEAMDKVGKEGVITVEDGT
GLQDELDVVEGMQFDRGYLSPYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVA
KAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVI
SEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQQIEEATSDYD
REKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGVVAGGGVALIR
VASKLADLRGQNEDQNVGIKVALRAMEAPLRQIVLNCGEEPSVVANTVKGGDGNYGYNAA
TEEYGNMIDMGILDPTKVTRSALQYAASVAGLMITTECMVTDLPKNDAADLGAAGGMGGM
GGMGGMM

Primary citation

Unmasking GroEL: Structure, dynamics, and substrate binding revealed by single-particle cryo-EM. Stapleton, K.M., Mizobata, T., Miyazaki, N. et al. To be published.

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

About this viewer

MolViewer shows 7XOK directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.