1KP8: GroEL protein

Structural Basis for GroEL-assisted Protein Folding from the Crystal Structure of (GroEL-KMgATP)14 at 2.0 A Resolution. Determined by X-ray diffraction at 2.0 Å resolution. Released 25 Mar 2003.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Escherichia coli
Chains: 14
Atoms: 57,085
Mol. weight: 810.23 kDa
Ligands: AGS, MG
Released: 25 Mar 2003

Explore 1KP8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1KP8 contains 359 α-helices and 372 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.

Chain A: 27 helices, 27 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
α-helix	47	1
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
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	174-178	5	4
β-strand	186-190	5	4
β-strand	193-195	3	5
β-strand	199	1	6
β-strand	207	1	7
β-strand	212	1	7
β-strand	213-216	4	5
β-strand	219-221	3	6
β-strand	223-224	2	8
β-strand	226-227	2	9
α-helix	230-232	3
α-helix	234-241	8
α-helix	242-244	3
β-strand	247-251	5	6
β-strand	253-254	2	9
α-helix	256-265	10
α-helix	266-268	3
β-strand	273-277	5	6
α-helix	278	1
α-helix	282-296	15
β-strand	301-302	2	8
α-helix	303-305	3
β-strand	318-319	2	6
β-strand	320-325	6	5
β-strand	330-335	6	5
α-helix	339-354	16
α-helix	359-374	16
β-strand	376-380	5	4
α-helix	386-409	24
β-strand	411-413	3	3
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	10
β-strand	484-487	4	10
β-strand	494-496	3	3
α-helix	497-515	19
β-strand	517-523	7	1

Chain B: 25 helices, 27 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	11
α-helix	47	1
β-strand	48-50	3	11
α-helix	53-58	6
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	175-178	4	13
β-strand	186-190	5	13
β-strand	193-195	3	14
β-strand	199	1	15
β-strand	207	1	16
β-strand	212	1	16
β-strand	213-216	4	14
β-strand	219-221	3	15
β-strand	223-224	2	17
β-strand	226-227	2	18
α-helix	230-232	3
α-helix	234-241	8
α-helix	242-244	3
β-strand	247-251	5	15
β-strand	253-254	2	18
α-helix	256-265	10
α-helix	266-268	3
β-strand	273-277	5	15
α-helix	278	1
α-helix	282-296	15
β-strand	301-302	2	17
α-helix	303-305	3
β-strand	318-319	2	15
β-strand	320-325	6	14
β-strand	330-335	6	14
α-helix	339-352	14
α-helix	359-374	16
β-strand	376-380	5	13
α-helix	386-409	24
β-strand	411-413	3	12
α-helix	417-423	7
α-helix	434-446	13
α-helix	449-458	10
α-helix	462-471	10
β-strand	476-479	4	19
β-strand	484-487	4	19
β-strand	494-496	3	12
α-helix	497-515	19
β-strand	517-523	7	2

Chain C: 26 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	11
α-helix	9-28	20
α-helix	35-36	2
β-strand	37-40	4	20
α-helix	47	1
β-strand	48-50	3	20
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	21
α-helix	137	1
α-helix	141-151	11
α-helix	156-169	14
β-strand	175-178	4	22
β-strand	186-190	5	22
β-strand	193-195	3	23
β-strand	199	1	24
β-strand	207	1	25
β-strand	212	1	25
β-strand	213-216	4	23
β-strand	219-221	3	24
β-strand	223-224	2	26
β-strand	226-227	2	27
α-helix	230-232	3
α-helix	234-241	8
β-strand	247-251	5	24
β-strand	253-254	2	27
α-helix	256-265	10
α-helix	266-268	3
β-strand	273-277	5	24
α-helix	278	1
α-helix	282-296	15
β-strand	301-302	2	26
α-helix	303-305	3
β-strand	318-319	2	24
β-strand	320-325	6	23
β-strand	330-335	6	23
α-helix	339-352	14
α-helix	359-374	16
β-strand	376-380	5	22
α-helix	386-409	24
β-strand	411-413	3	21
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	28
β-strand	484-487	4	28
β-strand	494-496	3	21
α-helix	497-515	19
β-strand	517-523	7	11

Chain D: 26 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	20
α-helix	9-28	20
α-helix	35-36	2
β-strand	37-40	4	29
α-helix	47	1
β-strand	48-50	3	29
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	30
α-helix	137	1
α-helix	141-151	11
α-helix	156-169	14
β-strand	174-178	5	31
β-strand	186-190	5	31
β-strand	193-195	3	32
β-strand	199	1	33
β-strand	207	1	34
β-strand	212	1	34
β-strand	213-216	4	32
β-strand	219-227	9	33
α-helix	230-232	3
α-helix	234-241	8
β-strand	247-254	8	33
α-helix	256-265	10
α-helix	266-268	3
β-strand	273-277	5	33
α-helix	278	1
α-helix	283-296	14
β-strand	301-302	2	33
α-helix	303-305	3
β-strand	318-319	2	33
β-strand	320-325	6	32
β-strand	330-335	6	32
α-helix	339-355	17
α-helix	359-374	16
β-strand	376-380	5	31
α-helix	386-409	24
β-strand	411-413	3	30
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	35
β-strand	484-487	4	35
β-strand	494-496	3	30
α-helix	497-515	19
β-strand	517-523	7	20

Chain E: 24 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	29
α-helix	9-28	20
α-helix	35-36	2
β-strand	37-40	4	36
α-helix	47	1
β-strand	48-50	3	36
α-helix	53-59	7
α-helix	65-85	21
α-helix	89-108	20
α-helix	113-134	22
β-strand	136	1	37
α-helix	141-151	11
α-helix	156-169	14
β-strand	175-178	4	38
β-strand	186-190	5	38
β-strand	193-195	3	39
β-strand	199	1	40
β-strand	207	1	41
β-strand	212	1	41
β-strand	213-216	4	39
β-strand	219-221	3	40
β-strand	223-224	2	42
β-strand	226-227	2	43
α-helix	230-232	3
α-helix	234-241	8
β-strand	247-251	5	40
β-strand	253-254	2	43
α-helix	256-265	10
α-helix	266-268	3
β-strand	273-277	5	40
α-helix	278	1
α-helix	283-296	14
β-strand	301-302	2	42
α-helix	303-305	3
β-strand	318-319	2	40
β-strand	320-325	6	39
β-strand	330-335	6	39
α-helix	339-352	14
α-helix	359-374	16
β-strand	376-380	5	38
α-helix	386-409	24
β-strand	411-413	3	37
α-helix	417-424	8
α-helix	434-446	13
α-helix	449-458	10
α-helix	462-471	10
β-strand	476-479	4	44
β-strand	484-487	4	44
β-strand	494-496	3	37
α-helix	497-515	19
β-strand	517-523	7	29

Chain F: 25 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	36
α-helix	9-28	20
α-helix	35-36	2
β-strand	37-40	4	45
α-helix	47	1
β-strand	48-50	3	45
α-helix	53-59	7
α-helix	65-85	21
α-helix	89-108	20
α-helix	113-134	22
β-strand	136	1	46
α-helix	141-151	11
α-helix	156-169	14
β-strand	175-178	4	47
β-strand	186-190	5	47
β-strand	193-195	3	48
β-strand	199	1	49
β-strand	207	1	50
β-strand	212	1	50
β-strand	213-216	4	48
β-strand	219-221	3	49
β-strand	223-224	2	51
β-strand	226-227	2	52
α-helix	230-232	3
α-helix	234-241	8
α-helix	242-244	3
β-strand	247-251	5	49
β-strand	253-254	2	52
α-helix	256-265	10
α-helix	266-268	3
β-strand	273-277	5	49
α-helix	278	1
α-helix	282-296	15
β-strand	301-302	2	51
α-helix	303-305	3
β-strand	318-319	2	49
β-strand	320-325	6	48
β-strand	330-335	6	48
α-helix	339-352	14
α-helix	359-374	16
β-strand	376-380	5	47
α-helix	386-409	24
β-strand	411-413	3	46
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	53
β-strand	484-487	4	53
β-strand	494-496	3	46
α-helix	497-515	19
β-strand	517-523	7	36

Chain G: 26 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	45
α-helix	9-28	20
α-helix	35-36	2
β-strand	37-40	4	1
α-helix	47	1
β-strand	48-50	3	1
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	54
α-helix	137	1
α-helix	141-151	11
α-helix	156-169	14
β-strand	175-179	5	55
β-strand	186-190	5	55
β-strand	193-195	3	56
β-strand	199	1	57
β-strand	207	1	58
β-strand	212	1	58
β-strand	213-216	4	56
β-strand	219-227	9	57
α-helix	230-232	3
α-helix	234-241	8
β-strand	247-254	8	57
α-helix	256-265	10
α-helix	266-268	3
β-strand	273-277	5	57
α-helix	278	1
α-helix	282-296	15
β-strand	301-302	2	57
α-helix	303-305	3
β-strand	318-319	2	57
β-strand	320-325	6	56
β-strand	330-335	6	56
α-helix	339-355	17
α-helix	359-374	16
β-strand	376-381	6	55
α-helix	386-409	24
β-strand	411-413	3	54
α-helix	417-425	9
α-helix	434-446	13
α-helix	449-456	8
α-helix	462-471	10
β-strand	476-479	4	59
β-strand	484-487	4	59
β-strand	494-496	3	54
α-helix	497-515	19
β-strand	517-523	7	45

Chains H and K: 25 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	60
α-helix	9-28	20
α-helix	35-36	2
β-strand	37-40	4	61
α-helix	47	1
β-strand	48-50	3	61
α-helix	53-59	7
α-helix	65-85	21
α-helix	89-108	20
α-helix	113-134	22
β-strand	136	1	62
α-helix	141-151	11
α-helix	156-169	14
β-strand	175-178	4	63
β-strand	186-190	5	63
β-strand	193-195	3	64
β-strand	199	1	65
β-strand	207	1	66
β-strand	212	1	66
β-strand	213-216	4	64
β-strand	219-221	3	65
β-strand	223-224	2	67
β-strand	226-227	2	68
α-helix	230-232	3
α-helix	234-241	8
α-helix	242-244	3
β-strand	247-251	5	65
β-strand	253-254	2	68
α-helix	256-265	10
α-helix	266-268	3
β-strand	273-277	5	65
α-helix	278	1
α-helix	282-296	15
β-strand	301-302	2	67
α-helix	303-305	3
β-strand	318-319	2	65
β-strand	320-325	6	64
β-strand	330-335	6	64
α-helix	339-354	16
α-helix	359-374	16
β-strand	376-380	5	63
α-helix	386-409	24
β-strand	411-413	3	62
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	69
β-strand	484-487	4	69
β-strand	494-496	3	62
α-helix	497-515	19
β-strand	517-523	7	60

5 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
groEL protein	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

>1KP8_1 groEL protein (chains A, B, C, D, E, F, G, H, I, J, K, L, M, N)
AAKDVKFGNDAGVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIE
LEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIITEGLKAVAAGMNPMDLKRGID
KAVTVAVEELKALSVPCSDSKAIAQVGTISANSDETVGKLIAEAMDKVGKEGVITVEDGT
GLQDELDVVEGMQFDRGYLSPYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVA
KAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVI
SEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQQIEEATSDYD
REKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGVVAGGGVALIR
VASKLADLRGQNADQNVGIKVALRAMEAPLRQIVLNCGEEPSVVANTVKGGDGNYGYNAA
TEEYGNMIDMGILDPTKVTRSALQYAASVAGLMITTECMVTDLPKNDAADLGAAGGMGGM
GGMGGMM

Ligands and cofactors

ID	Name	Formula	Copies
AGS	Phosphothiophosphoric acid-adenylate ester	C10 H16 N5 O12 P3 S	14
MG	Magnesium ion	Mg	14

Water and common crystallization additives (SO4, K) are not listed.

Primary citation

Structural Basis for GroEL-assisted Protein Folding from the Crystal Structure of (GroEL-KMgATP)14 at 2.0 A Resolution. Wang, J., Boisvert, D.C. J Mol Biol (2003) 327:843-855. DOI 10.1016/S0022-2836(03)00184-0 · 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…
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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