1SS8: GroEL

GroEL. Determined by X-ray diffraction at 2.7 Å resolution. Released 1 Mar 2005.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Escherichia coli
Chains: 7
Atoms: 27,064
Mol. weight: 386.04 kDa
Released: 1 Mar 2005

Explore 1SS8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1SS8 contains 176 α-helices and 169 β-strands across 7 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.

Chain A: 26 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	1
α-helix	9-28	20
α-helix	35-36	2
β-strand	37-40	4	2
β-strand	48-50	3	2
α-helix	53-58	6
α-helix	65-85	21
α-helix	89-108	20
α-helix	113-134	22
α-helix	135	1
β-strand	136	1	3
α-helix	137	1
α-helix	141-151	11
α-helix	156-169	14
β-strand	174-179	6	4
β-strand	186-190	5	4
β-strand	192-195	4	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	219-227	9	6
α-helix	234-243	10
β-strand	247-254	8	6
α-helix	256-267	12
β-strand	273-277	5	6
α-helix	278	1
α-helix	282-296	15
β-strand	301-302	2	6
α-helix	303-305	3
α-helix	314-316	3
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	359-372	14
β-strand	376-381	6	4
α-helix	382	1
α-helix	386-409	24
β-strand	411-413	3	3
α-helix	417-424	8
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
β-strand	494-496	3	3
α-helix	497-515	19
β-strand	517-523	7	1

Chain B: 25 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	9
α-helix	9-28	20
α-helix	35-36	2
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	10
α-helix	141-151	11
α-helix	156-169	14
β-strand	174-179	6	11
β-strand	186-190	5	11
β-strand	192-195	4	12
β-strand	199	1	13
α-helix	202-204	3
β-strand	207	1	14
β-strand	212	1	14
β-strand	213-216	4	12
β-strand	219-227	9	13
α-helix	234-243	10
β-strand	247-254	8	13
α-helix	256-267	12
β-strand	273-277	5	13
α-helix	278	1
α-helix	282-296	15
β-strand	301-302	2	13
α-helix	303-305	3
α-helix	314-316	3
β-strand	318-319	2	13
β-strand	320-325	6	12
β-strand	330-335	6	12
α-helix	339-355	17
α-helix	359-374	16
β-strand	376-381	6	11
α-helix	382	1
α-helix	386-409	24
β-strand	411-413	3	10
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	15
β-strand	484-487	4	15
α-helix	488-491	4
β-strand	494-496	3	10
α-helix	497-515	19
β-strand	517-523	7	9

Chain C: 24 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	16
α-helix	9-28	20
α-helix	35-36	2
β-strand	37-40	4	9
α-helix	47	1
β-strand	48-50	3	9
α-helix	53-59	7
α-helix	65-85	21
α-helix	89-108	20
α-helix	113-134	22
β-strand	136	1	17
α-helix	141-151	11
α-helix	156-169	14
β-strand	174-179	6	18
β-strand	186-190	5	18
β-strand	192-195	4	19
β-strand	199	1	20
α-helix	202-204	3
β-strand	207	1	21
β-strand	212	1	21
β-strand	213-216	4	19
β-strand	219-227	9	20
α-helix	234-243	10
β-strand	247-254	8	20
α-helix	256-267	12
β-strand	273-277	5	20
α-helix	278	1
α-helix	282-296	15
β-strand	301-302	2	20
α-helix	303-305	3
α-helix	314-316	3
β-strand	318-319	2	20
β-strand	320-325	6	19
β-strand	330-335	6	19
α-helix	339-355	17
α-helix	359-372	14
β-strand	376-381	6	18
α-helix	386-409	24
β-strand	411-413	3	17
α-helix	417-425	9
α-helix	434-446	13
α-helix	449-457	9
α-helix	462-471	10
β-strand	476-479	4	22
β-strand	484-487	4	22
β-strand	494-496	3	17
α-helix	497-515	19
β-strand	517-523	7	16

Chain D: 26 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	23
α-helix	9-28	20
α-helix	35-36	2
β-strand	37-40	4	16
α-helix	47	1
β-strand	48-50	3	16
α-helix	53-58	6
α-helix	65-85	21
α-helix	89-108	20
α-helix	113-134	22
α-helix	135	1
β-strand	136	1	24
α-helix	137	1
α-helix	141-151	11
α-helix	156-169	14
β-strand	175-179	5	25
β-strand	186-190	5	25
β-strand	192-195	4	26
β-strand	199	1	27
α-helix	202-204	3
β-strand	207	1	28
β-strand	212	1	28
β-strand	213-216	4	26
β-strand	219-227	9	27
α-helix	234-243	10
β-strand	247-254	8	27
α-helix	256-267	12
β-strand	273-277	5	27
α-helix	278	1
α-helix	282-296	15
β-strand	301-302	2	27
α-helix	303-305	3
α-helix	314-316	3
β-strand	318-319	2	27
β-strand	320-325	6	26
β-strand	330-335	6	26
α-helix	339-355	17
α-helix	359-374	16
β-strand	376-381	6	25
α-helix	386-409	24
β-strand	411-413	3	24
α-helix	417-425	9
α-helix	434-446	13
α-helix	449-457	9
α-helix	462-471	10
β-strand	476-479	4	29
β-strand	484-487	4	29
β-strand	494-496	3	24
α-helix	497-515	19
β-strand	517-523	7	23

Chain E: 25 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	30
α-helix	9-28	20
α-helix	35-36	2
β-strand	37-40	4	23
β-strand	48-50	3	23
α-helix	53-59	7
α-helix	65-85	21
α-helix	89-108	20
α-helix	113-134	22
α-helix	135	1
β-strand	136	1	31
α-helix	137	1
α-helix	141-151	11
α-helix	156-169	14
β-strand	175-179	5	32
β-strand	186-190	5	32
β-strand	192-195	4	33
β-strand	199	1	34
α-helix	202-204	3
β-strand	207	1	35
β-strand	212	1	35
β-strand	213-216	4	33
β-strand	219-227	9	34
α-helix	234-243	10
β-strand	247-254	8	34
α-helix	256-267	12
β-strand	273-277	5	34
α-helix	278	1
α-helix	282-296	15
β-strand	301-302	2	34
α-helix	303-305	3
α-helix	314-316	3
β-strand	318-319	2	34
β-strand	320-325	6	33
β-strand	330-335	6	33
α-helix	339-355	17
α-helix	359-374	16
β-strand	376-381	6	32
α-helix	386-409	24
β-strand	411-413	3	31
α-helix	417-425	9
α-helix	434-446	13
α-helix	449-457	9
α-helix	462-471	10
β-strand	476-479	4	36
β-strand	484-487	4	36
β-strand	494-496	3	31
α-helix	497-515	19
β-strand	517-523	7	30

Chain F: 25 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	37
α-helix	9-28	20
α-helix	35-36	2
β-strand	37-40	4	30
β-strand	48-50	3	30
α-helix	53-59	7
β-strand	62	1	30
α-helix	65-85	21
α-helix	89-108	20
α-helix	113-134	22
α-helix	135	1
β-strand	136	1	38
α-helix	137	1
α-helix	141-151	11
α-helix	156-169	14
β-strand	174-179	6	39
β-strand	186-190	5	39
β-strand	192-195	4	40
β-strand	199	1	41
α-helix	202-204	3
β-strand	207	1	42
β-strand	212	1	42
β-strand	213-216	4	40
β-strand	219-227	9	41
α-helix	234-243	10
β-strand	247-254	8	41
α-helix	256-267	12
β-strand	273-277	5	41
α-helix	278	1
α-helix	282-296	15
β-strand	301-302	2	41
α-helix	303-305	3
α-helix	314-316	3
β-strand	318-319	2	41
β-strand	320-325	6	40
β-strand	330-335	6	40
α-helix	339-355	17
α-helix	359-374	16
β-strand	376-381	6	39
α-helix	386-409	24
β-strand	411-413	3	38
α-helix	417-425	9
α-helix	434-446	13
α-helix	449-457	9
α-helix	462-471	10
β-strand	476-479	4	43
β-strand	484-487	4	43
β-strand	494-496	3	38
α-helix	497-515	19
β-strand	517-523	7	37

Chain G: 25 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	2
α-helix	9-28	20
α-helix	35-36	2
β-strand	37-40	4	37
β-strand	48-50	3	37
α-helix	53-58	6
α-helix	65-85	21
α-helix	89-108	20
α-helix	113-134	22
α-helix	135	1
β-strand	136	1	44
α-helix	137	1
α-helix	141-151	11
α-helix	156-169	14
β-strand	174-179	6	45
β-strand	186-190	5	45
β-strand	192-195	4	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	219-227	9	47
α-helix	234-243	10
β-strand	247-254	8	47
α-helix	256-267	12
β-strand	273-277	5	47
α-helix	278	1
α-helix	282-296	15
β-strand	301-302	2	47
α-helix	303-305	3
α-helix	314-316	3
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	359-374	16
β-strand	376-381	6	45
α-helix	386-409	24
β-strand	411-413	3	44
α-helix	417-425	9
α-helix	434-446	13
α-helix	449-457	9
α-helix	462-471	10
β-strand	476-479	4	49
β-strand	484-487	4	49
β-strand	494-496	3	44
α-helix	497-515	19
β-strand	517-523	7	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
groEL protein	A, B, C, D, E, F, G	protein	524	Escherichia coli	P0A6F5 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G), FASTA

>1SS8_1 groEL protein (chains A, B, C, D, E, F, G)
AAKDVKFGNDAGVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIE
LEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIITEGLKAVAAGMNPMDLKRGID
KAVTVAVEELKALSVPCSDSKAIAQVGTISANSDETVGKLIAEAMDKVGKEGVITVEDGT
GLQDELDVVEGMQFDRGYLSPYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVA
KAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVI
SEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQQIEEATSDYD
REKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGVVAGGGVALIR
VASKLADLRGQNEDQNVGIKVALRAMEAPLRQIVLNCGEEPSVVANTVKGGDGNYGYNAA
TEEYGNMIDMGILDPTKVTRSALQYAASVAGLMITTECMVTDLP

Primary citation

Exploring the structural dynamics of the E.coli chaperonin GroEL using translation-libration-screw crystallographic refinement of intermediate states. Chaudhry, C., Horwich, A.L., Brunger, A.T. et al. J Mol Biol (2004) 342:229-245. DOI 10.1016/j.jmb.2004.07.015 · 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

About this viewer

MolViewer shows 1SS8 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.