1OEL: Groel

Name: PDB 1OEL: Conformational variability in the refined structure of the chaperonin groel at 2.8 Å resolution
Published: 1996-04-03
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperonin

Conformational variability in the refined structure of the chaperonin groel at 2.8 Å resolution. Determined by X-ray diffraction at 2.8 Å resolution. Released 3 Apr 1996.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Escherichia coli
Chains: 7
Atoms: 27,078
Mol. weight: 399.9 kDa
Released: 3 Apr 1996

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

Secondary structure: helices and β-sheets

1OEL contains 204 α-helices and 168 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.

Chains A and E: 30 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	53-59	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	174-179	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	213-216	4	5
α-helix	218	1
β-strand	219-227	9	6
α-helix	231-233	3
α-helix	234-243	10
β-strand	247-254	8	6
α-helix	259-261	3
α-helix	262-266	5
β-strand	273-277	5	6
α-helix	278	1
α-helix	282-296	15
β-strand	300-301	2	6
α-helix	303-305	3
α-helix	309-311	3
α-helix	314-316	3
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	339-354	16
α-helix	359-374	16
β-strand	376-381	6	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	462-471	10
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

Chains B, C and G: 28 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	53-59	7
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	193-195	3	12
β-strand	199	1	13
α-helix	202-204	3
β-strand	213-216	4	12
α-helix	218	1
β-strand	219-227	9	13
α-helix	231-233	3
α-helix	234-243	10
β-strand	247-254	8	13
α-helix	259-261	3
α-helix	262-266	5
β-strand	273-277	5	13
α-helix	278	1
α-helix	282-296	15
β-strand	300-301	2	13
α-helix	303-305	3
α-helix	309-311	3
α-helix	314-316	3
β-strand	318-319	2	13
β-strand	320	1	14
β-strand	322-325	4	12
β-strand	330-332	3	12
β-strand	335	1	14
α-helix	339-354	16
α-helix	359-374	16
β-strand	376-381	6	11
α-helix	386-409	24
β-strand	411-413	3	10
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	15
β-strand	484-487	4	15
β-strand	494-496	3	10
α-helix	497-515	19
β-strand	517-523	7	9

Chain D: 31 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	23
α-helix	9-27	19
α-helix	28-30	3
α-helix	35-36	2
β-strand	37-40	4	16
β-strand	48-50	3	16
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	24
α-helix	137	1
α-helix	141-151	11
α-helix	156-169	14
β-strand	174-179	6	25
β-strand	186-190	5	25
β-strand	193-195	3	26
β-strand	199	1	27
α-helix	202-204	3
β-strand	213-216	4	26
α-helix	218	1
β-strand	219-227	9	27
α-helix	231-233	3
α-helix	234-243	10
β-strand	247-254	8	27
α-helix	259-261	3
α-helix	262-266	5
β-strand	273-277	5	27
α-helix	278	1
α-helix	282-296	15
β-strand	300-301	2	27
α-helix	303-305	3
α-helix	309-311	3
α-helix	314-316	3
β-strand	318-319	2	27
β-strand	320	1	28
β-strand	322-325	4	26
β-strand	330-332	3	26
β-strand	335	1	28
α-helix	339-354	16
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	426-428	3
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 F: 29 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	4-8	5	37
α-helix	9-27	19
α-helix	28-30	3
α-helix	35-36	2
β-strand	37-40	4	30
β-strand	48-50	3	30
α-helix	53-59	7
α-helix	65-85	21
α-helix	89-108	20
α-helix	113-134	22
β-strand	136	1	38
α-helix	141-151	11
α-helix	156-169	14
β-strand	174-179	6	39
β-strand	186-190	5	39
β-strand	193-195	3	40
β-strand	199	1	41
α-helix	202-204	3
β-strand	213-216	4	40
α-helix	218	1
β-strand	219-227	9	41
α-helix	231-233	3
α-helix	234-243	10
β-strand	247-254	8	41
α-helix	259-261	3
α-helix	262-266	5
β-strand	273-277	5	41
α-helix	278	1
α-helix	282-296	15
β-strand	300-301	2	41
α-helix	303-305	3
α-helix	309-311	3
α-helix	314-316	3
β-strand	318-319	2	41
β-strand	320	1	42
β-strand	322-325	4	40
β-strand	330-332	3	40
β-strand	335	1	42
α-helix	339-354	16
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	426-428	3
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

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Groel (HSP60 class)	A, B, C, D, E, F, G	protein	547	Escherichia coli	P0A6F5 (AlphaFold model)

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

>1OEL_1 GROEL (HSP60 CLASS) (chains A, B, C, D, E, F, G)
AAKDVKFGNDAGVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIE
LEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIITEGLKAVAAGMNPMDLKRGID
KAVTVAVEELKALSVPCSDSKAIAQVGTISANSDETVGKLIAEAMDKVGKEGVITVEDGT
GLQDELDVVEGMQFDRGYLSPYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVA
KAGKPLLIIAEDVEGEALATAVVNTIRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVI
SEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQQIEEATSDYD
REKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGVVAGGGVALIR
VASKLADLRGQNEDQNVGIKVALRAMEAPLRQIVLNCGEEPSVVANTVKGGDGNYGYNAA
TEEYGNMIDMGILDPTKVTRSALQYAASVAGLMITTECMVTDLPKNDAADLGAAGGMGGM
GGMGGMM

Primary citation

Conformational variability in the refined structure of the chaperonin GroEL at 2.8 A resolution. Braig, K., Adams, P.D., Brunger, A.T. Nat Struct Biol (1995) 2:1083-1094. DOI 10.1038/nsb1295-1083 · 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

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1OEL is part of these collections:

Protein folding, misfolding and amyloid

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