3BTU: PDB entry 3BTU

Crystal structure of the super-repressor mutant of Gal80p from Saccharomyces cerevisiae; Gal80(S2) [E351K]. Determined by X-ray diffraction at 2.85 Å resolution. Released 4 Mar 2008.

Method: X-ray diffraction
Resolution: 2.85 Å
Organism: Saccharomyces cerevisiae
Chains: 6
Atoms: 18,389
Mol. weight: 291.93 kDa
Released: 4 Mar 2008

Explore 3BTU in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3BTU contains 112 α-helices and 133 β-strands across 6 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: 19 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	18-23	6	1
α-helix	32-34	3
α-helix	36-42	7
β-strand	47-53	7	1
α-helix	57-66	10
β-strand	73-74	2	1
α-helix	78-83	6
β-strand	89-92	4	1
α-helix	96-98	3
α-helix	99-109	11
α-helix	110-112	3
β-strand	118-121	4	1
α-helix	122	1
α-helix	129-142	14
β-strand	145-148	4	1
α-helix	151-154	4
α-helix	156-166	11
β-strand	173-181	9	2
β-strand	188-190	3	3
α-helix	195-198	4
α-helix	206-211	6
α-helix	212-221	10
β-strand	226-229	4	2
β-strand	232-234	3	2
β-strand	239-243	5	3
β-strand	249-255	7	3
β-strand	261-268	8	2
β-strand	273-280	8	2
α-helix	285-286	2
β-strand	292-298	7	2
β-strand	302-307	6	2
α-helix	312-314	3
β-strand	318-321	4	2
β-strand	351-353	3	2
α-helix	360-377	18
α-helix	402-421	20
β-strand	423	1	4
β-strand	425-426	2	2
α-helix	428-431	4

Chain B: 20 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	17	1
β-strand	18-23	6	5
α-helix	32-34	3
α-helix	36-42	7
β-strand	47-53	7	5
α-helix	57-66	10
β-strand	73-74	2	5
α-helix	78-83	6
β-strand	89-92	4	5
α-helix	96-98	3
α-helix	99-109	11
α-helix	110-112	3
β-strand	118-121	4	5
α-helix	122	1
α-helix	129-142	14
β-strand	145-148	4	5
α-helix	151-154	4
α-helix	156-166	11
β-strand	173-181	9	6
β-strand	188-190	3	7
α-helix	195-198	4
α-helix	206-211	6
α-helix	212-222	11
β-strand	226-229	4	6
β-strand	232-234	3	6
β-strand	239-243	5	7
β-strand	249-255	7	7
β-strand	261-268	8	6
β-strand	273-280	8	6
α-helix	285-286	2
β-strand	292-298	7	6
β-strand	302-307	6	6
α-helix	312-314	3
β-strand	318-321	4	6
β-strand	352-353	2	6
α-helix	360-376	17
α-helix	402-421	20
β-strand	423	1	4
β-strand	425-426	2	6
α-helix	428-431	4

Chain C: 20 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	17	1
β-strand	18-23	6	8
α-helix	32-34	3
α-helix	36-41	6
β-strand	47-53	7	8
α-helix	57-66	10
β-strand	73-74	2	8
α-helix	78-83	6
β-strand	89-92	4	8
α-helix	96-98	3
α-helix	99-109	11
α-helix	110-112	3
β-strand	118-121	4	8
α-helix	122	1
α-helix	129-142	14
β-strand	145-148	4	8
α-helix	151-154	4
α-helix	156-166	11
β-strand	173-181	9	9
β-strand	188-190	3	10
α-helix	195-198	4
α-helix	206-211	6
α-helix	212-222	11
β-strand	226-229	4	9
β-strand	232-234	3	9
β-strand	239-243	5	10
β-strand	249-255	7	10
β-strand	261-268	8	9
β-strand	273-280	8	9
α-helix	285-286	2
β-strand	292-298	7	9
β-strand	302-307	6	9
α-helix	312-314	3
β-strand	318-321	4	9
β-strand	351-353	3	9
α-helix	360-376	17
α-helix	402-421	20
β-strand	423	1	11
β-strand	425-426	2	9
α-helix	428-431	4

Chain D: 19 helices, 20 β-strands

Element	Residues	Length	Sheet
α-helix	17	1
β-strand	18-23	6	12
α-helix	32-34	3
α-helix	36-42	7
β-strand	47-53	7	12
α-helix	57-66	10
β-strand	73-74	2	12
α-helix	78-83	6
β-strand	89-92	4	12
α-helix	96-98	3
α-helix	99-109	11
α-helix	110-112	3
β-strand	118-121	4	12
α-helix	129-142	14
β-strand	145-148	4	12
α-helix	151-154	4
α-helix	156-166	11
β-strand	173-181	9	13
β-strand	188-190	3	14
α-helix	195-198	4
α-helix	206-211	6
α-helix	212-222	11
β-strand	226-229	4	13
β-strand	232-234	3	13
β-strand	239-243	5	14
β-strand	249-255	7	14
β-strand	261-268	8	13
β-strand	273-280	8	13
α-helix	285-286	2
β-strand	292-298	7	13
β-strand	302-307	6	13
α-helix	312-314	3
β-strand	318-321	4	13
β-strand	351-353	3	13
α-helix	360-376	17
α-helix	402-421	20
β-strand	423	1	11
β-strand	425-426	2	13
α-helix	428-431	4

Chain E: 17 helices, 27 β-strands

Element	Residues	Length	Sheet
β-strand	18-23	6	15
α-helix	37-40	4
β-strand	47-53	7	15
α-helix	57-66	10
β-strand	73-75	3	15
α-helix	78-83	6
β-strand	89-92	4	15
α-helix	96-98	3
α-helix	99-109	11
α-helix	110-112	3
β-strand	118-121	4	15
α-helix	129-142	14
β-strand	145-148	4	15
α-helix	151-153	3
α-helix	156-167	12
β-strand	176	1	16
β-strand	178-179	2	17
β-strand	181	1	18
β-strand	184	1	19
β-strand	188-190	3	20
α-helix	195-197	3
α-helix	206-211	6
α-helix	212-222	11
β-strand	226-229	4	16
β-strand	232-234	3	18
β-strand	239-243	5	20
β-strand	249-255	7	20
β-strand	261-263	3	18
β-strand	265-268	4	16
α-helix	270-272	3
β-strand	273-276	4	16
β-strand	280	1	18
β-strand	282	1	19
α-helix	285-286	2
β-strand	293-294	2	17
β-strand	303	1	21
α-helix	312-314	3
β-strand	318	1	22
β-strand	321	1	21
β-strand	354	1	22
α-helix	360-376	17
α-helix	402-421	20
β-strand	423	1	23
β-strand	425-426	2	16

Chain F: 17 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	18-23	6	24
α-helix	37-40	4
β-strand	47-53	7	24
α-helix	57-66	10
β-strand	73-75	3	24
α-helix	78-83	6
β-strand	89-92	4	24
α-helix	96-98	3
α-helix	99-109	11
α-helix	110-112	3
β-strand	118-121	4	24
α-helix	129-142	14
β-strand	145-148	4	24
α-helix	151-154	4
α-helix	156-166	11
β-strand	176-177	2	25
β-strand	178-179	2	26
β-strand	180-181	2	27
β-strand	184	1	28
β-strand	188-190	3	29
α-helix	195-197	3
α-helix	206-211	6
α-helix	212-222	11
β-strand	226-229	4	25
β-strand	232-234	3	27
β-strand	239-243	5	29
β-strand	249-255	7	29
β-strand	261-263	3	27
β-strand	265-268	4	25
α-helix	270-272	3
β-strand	273-276	4	25
β-strand	279-280	2	27
β-strand	282	1	28
α-helix	285-286	2
β-strand	292-294	3	26
β-strand	304-307	4	26
α-helix	312-314	3
β-strand	318-320	3	26
β-strand	354	1	26
α-helix	360-376	17
α-helix	402-421	20
β-strand	423	1	23
β-strand	425-426	2	25

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Galactose/lactose metabolism regulatory protein GAL80	A, B, C, D, E, F	protein	438	Saccharomyces cerevisiae	P04387 (AlphaFold model)

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

>3BTU_1 Galactose/lactose metabolism regulatory protein GAL80 (chains A, B, C, D, E, F)
GSHMDYNKRSSVSTVPNAAPIRVGFVGLNAAKGWAIKTHYPAILQLSSQFQITALYSPKI
ETSIATIQRLKLSNATAFPTLESFASSSTIDMIVIAIQVASHYEVVMPLLEFSKNNPNLK
YLFVEWALACSLDQAESIYKAAAERGVQTIISLQGRKSPYILRAKELISQGYIGDINSIE
IAGNGGWYGYERPVKSPKYIYEIGNGVDLVTTTFGHTIDILQYMTSSYFSRINAMVFNNI
PEQELIDERGNRLGQRVPKTVPDHLLFQGTLLNGNVPVSCSFKGGKPTKKFTKNLVIDIH
GTKGDLKLEGDAGFAEISNLVLYYSGTRANDFPLANGQQAPLDPGYDAGKEIMKVYHLRN
YNAIVGNIHRLYQSISDFHFNTKKIPELPSQFVMQGFDFEGFPTLMDALILHRLIESVYK
SNMMGSTLNVSNISHYSL

Primary citation

NADP regulates the yeast GAL induction system. Kumar, P.R., Yu, Y., Sternglanz, R. et al. Science (2008) 319:1090-1092. DOI 10.1126/science.1151903 · PubMed

Other PDB entries of the same protein (UniProt P04387 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3BTV 2.1 Å, Crystal structure of the super-repressor mutant of Gal80p from Saccharomyces cerevisiae;…
3V2U 2.1 Å, Crystal structure of the yeast GAL regulon complex of the repressor, Gal80p, and the…
3BTS 2.7 Å, Crystal structure of a ternary complex of the transcriptional repressor Gal80p (Gal80S0…

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