5TKY: Putative uncharacterized protein

Name: PDB 5TKY: Crystal structure of the co-translational Hsp70 chaperone Ssb in the ATP-bound, open conformation
Published: 2016-11-16
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: chaperone

Crystal structure of the co-translational Hsp70 chaperone Ssb in the ATP-bound, open conformation. Determined by X-ray diffraction at 2.6 Å resolution. Released 16 Nov 2016.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
Chains: 2
Atoms: 9,273
Mol. weight: 136.92 kDa
Ligands: MG, ATP
Released: 16 Nov 2016

Explore 5TKY in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5TKY contains 45 α-helices and 72 β-strands across 2 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: 23 helices, 35 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	1
β-strand	10-14	5	2
β-strand	18-24	7	2
β-strand	29-31	3	2
α-helix	32-33	2
β-strand	41-42	2	2
β-strand	44-47	4	3
β-strand	52-54	3	3
α-helix	56-60	5
β-strand	69-71	3	3
α-helix	73-75	3
α-helix	84-92	9
β-strand	96-100	5	4
β-strand	103-110	8	4
β-strand	113-117	5	4
α-helix	119-138	20
β-strand	141	1	1
β-strand	144-149	6	2
α-helix	155-167	13
β-strand	171-177	7	2
α-helix	178-184	7
α-helix	185-190	6
β-strand	197-204	8	5
β-strand	209-217	9	5
β-strand	220-229	10	5
α-helix	234-253	20
α-helix	261-278	18
β-strand	283-292	10	6
β-strand	295-302	8	6
α-helix	303-309	7
α-helix	311-316	6
α-helix	318-328	11
α-helix	332-334	3
β-strand	337-341	5	5
α-helix	343-346	4
α-helix	348-357	10
α-helix	361-363	3
β-strand	364	1	5
α-helix	372-384	13
β-strand	397-399	3	5
β-strand	401	1	7
β-strand	406-409	4	8
β-strand	414	1	9
β-strand	415-419	5	8
β-strand	424	1	7
β-strand	427-433	7	10
β-strand	443-449	7	8
β-strand	454	1	9
α-helix	455-457	3
β-strand	459-466	8	8
β-strand	479-485	7	10
β-strand	491-497	7	10
β-strand	501-503	3	10
α-helix	504-505	2
β-strand	506-509	4	8
α-helix	517-558	42
α-helix	573-587	15
α-helix	593-611	19

Chain B: 22 helices, 37 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	11
β-strand	10-14	5	12
β-strand	18-24	7	12
β-strand	29-31	3	12
α-helix	32-33	2
β-strand	41-42	2	12
β-strand	45-47	3	13
β-strand	52-54	3	13
α-helix	56-60	5
α-helix	66-68	3
β-strand	69-70	2	13
α-helix	73-75	3
α-helix	84-92	9
β-strand	96-100	5	14
β-strand	103-110	8	14
β-strand	113-117	5	14
α-helix	119-138	20
β-strand	141	1	11
β-strand	144-149	6	12
α-helix	155-167	13
β-strand	171-177	7	12
α-helix	178-188	11
β-strand	197-204	8	15
β-strand	209-217	9	15
β-strand	220-229	10	15
α-helix	234-253	20
α-helix	261-278	18
β-strand	283-288	6	16
β-strand	291	1	17
β-strand	295	1	17
β-strand	297-302	6	16
α-helix	303-309	7
α-helix	311-316	6
α-helix	318-327	10
α-helix	332-334	3
β-strand	337-341	5	15
α-helix	343-346	4
α-helix	348-357	10
α-helix	361-363	3
β-strand	364	1	15
α-helix	372-384	13
β-strand	397-399	3	15
β-strand	401	1	18
β-strand	405-409	5	19
β-strand	414	1	20
β-strand	415-419	5	19
β-strand	424	1	18
β-strand	427-433	7	21
β-strand	443-450	8	19
β-strand	454	1	20
α-helix	455-457	3
β-strand	459-466	8	19
β-strand	479-485	7	21
β-strand	491-497	7	21
β-strand	504	1	21
β-strand	506-509	4	19
α-helix	517-558	42
α-helix	571-587	17
α-helix	593-611	19

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Putative uncharacterized protein	A, B	protein	621	Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)	G0SCU5 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5TKY_1 Putative uncharacterized protein (chains A, B)
MGHHHHHHAEEVYDGAIGIDLGTTYSCVAVYEGTNVEIIANEQGNFTTPSFVSFTENCRL
IGEAAKNQAAMNPANTIFDVKRLIGRRFDDPTVKKDMESWPFKVVDDNGNPKVEVQYLGQ
THTFSPQEISAMVLTKMKEIAETKLGKKVEKAVITVPAYFNDNQRQATKDAGAIAGLNVL
RIINEPTAAAIAYGLGSGKSDKERNVLIYDLGGGAFDVSLLNIQGGVFTVKATAGDTHLG
GQDFDTNLLEYCKKEFTRKTKKDLSGDARALRRLRTACERAKRTLSSGAQTTIEIDSLFD
GEDFNIQITRARFEDLNAKAFAGTLEPVAQVLKDAGIEKHQVDEIVLVGGSTRIPRIQKL
LSEFFDGKKLEKSINPDEAVAYGAAVQAGILSGKATSADTSDLLLLDVVPLSLGVAMEGN
IFAPVVPRGQTVPTIKKRTFTTVADNQQTVQFPVYQGERVNCEDNTLLGEFTLAPIPPMK
AGEPVLEVVFEVDVNGILKVTATEKTSGRSANITIANSVGKLSTDEIEKMISDAEKFKSK
CEAFSKRFEAKQQLESYISRVEEIISDPTLSLKLKRGQKDKIEQALSEAMAQLEIEDSTA
DELKKKELALKRLVTKAMASR

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	2
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	2

Primary citation

Interaction of the cotranslational Hsp70 Ssb with ribosomal proteins and rRNA depends on its lid domain. Gumiero, A., Conz, C., Gese, G.V. et al. Nat Commun (2016) 7:13563-13563. DOI 10.1038/ncomms13563 · PubMed

Other PDB entries of the same protein (UniProt G0SCU5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7OLC 2.9 Å, Thermophilic eukaryotic 80S ribosome at idle POST state
8OO0 3.1 Å, Chaetomium thermophilum Methionine Aminopeptidase 2 autoproteolysis product at the 80S…

Browse structure collections

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