3V2U: PDB entry 3V2U

Crystal structure of the yeast GAL regulon complex of the repressor, Gal80p, and the transducer, Gal3p, with galactose and ATP. Determined by X-ray diffraction at 2.1 Å resolution. Released 8 Feb 2012.

Method: X-ray diffraction
Resolution: 2.1 Å
Organism: Saccharomyces cerevisiae
Chains: 4
Atoms: 15,960
Mol. weight: 215.22 kDa
Ligands: ATP, GLA, MG
Released: 8 Feb 2012

Explore 3V2U in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3V2U contains 93 α-helices and 88 β-strands across 4 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: 18 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	16-17	2
β-strand	18-23	6	1
α-helix	31-34	4
α-helix	36-41	6
β-strand	47-53	7	1
α-helix	57-66	10
β-strand	73-75	3	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	118-122	5	1
α-helix	129-142	14
β-strand	145-149	5	1
α-helix	151-154	4
α-helix	156-166	11
β-strand	173-181	9	2
β-strand	184	1	3
β-strand	188-190	3	4
α-helix	195-198	4
α-helix	206-211	6
α-helix	212-222	11
β-strand	226-234	9	2
β-strand	239-243	5	4
β-strand	249-255	7	4
β-strand	261-268	8	2
β-strand	273-280	8	2
β-strand	282	1	3
α-helix	285-286	2
β-strand	292-298	7	2
β-strand	301-307	7	2
α-helix	312-314	3
β-strand	318-323	6	2
β-strand	349-353	5	2
α-helix	360-376	17
α-helix	402-421	20
β-strand	423	1	5
β-strand	425-426	2	2

Chain B: 18 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	16-17	2
β-strand	18-23	6	6
β-strand	26	1	7
β-strand	29	1	7
α-helix	31-34	4
α-helix	36-42	7
β-strand	47-53	7	6
α-helix	57-66	10
β-strand	73-75	3	6
α-helix	78-83	6
β-strand	89-92	4	6
α-helix	96-98	3
α-helix	99-109	11
α-helix	110-112	3
β-strand	118-122	5	6
α-helix	129-142	14
β-strand	145-149	5	6
α-helix	151-154	4
α-helix	156-166	11
β-strand	173-181	9	8
β-strand	184	1	9
β-strand	188-190	3	10
α-helix	195-198	4
α-helix	206-211	6
α-helix	212-222	11
β-strand	226-234	9	8
β-strand	239-243	5	10
β-strand	249-255	7	10
β-strand	261-268	8	8
β-strand	273-280	8	8
β-strand	282	1	9
α-helix	285-286	2
β-strand	292-298	7	8
β-strand	301-307	7	8
α-helix	312-314	3
β-strand	318-323	6	8
β-strand	349-353	5	8
α-helix	360-376	17
α-helix	402-421	20
β-strand	423	1	5
β-strand	425-426	2	8

Chain C: 30 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	4	1	11
β-strand	7-8	2	12
α-helix	17-34	18
β-strand	40-51	12	12
α-helix	56-58	3
β-strand	62	1	13
β-strand	63-77	15	12
β-strand	84-89	6	12
β-strand	97-100	4	12
α-helix	101-102	2
α-helix	106-109	4
α-helix	117-135	19
α-helix	137-140	4
α-helix	144-147	4
β-strand	148-154	7	12
α-helix	156-157	2
α-helix	162-179	18
β-strand	186	1	11
α-helix	187-194	8
α-helix	197-201	5
α-helix	208-215	8
β-strand	217	1	14
β-strand	220	1	14
β-strand	221-225	5	13
β-strand	231-235	5	13
α-helix	236-240	5
β-strand	244-251	8	15
α-helix	254-256	3
α-helix	258-261	4
α-helix	266-283	18
β-strand	286	1	16
α-helix	287-289	3
α-helix	302-313	12
α-helix	318-319	2
α-helix	324-342	19
β-strand	349	1	17
α-helix	351-357	7
α-helix	362-365	4
α-helix	366-370	5
β-strand	375-377	3	8
β-strand	380	1	17
α-helix	382-403	22
α-helix	411-431	21
α-helix	438-449	12
β-strand	454-457	4	15
β-strand	465-472	8	15
α-helix	478-485	8
α-helix	486-490	5
α-helix	491-493	3
α-helix	499-505	7
β-strand	506-508	3	15
β-strand	516-519	4	12

Chain D: 27 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	4	1	18
β-strand	7-8	2	19
α-helix	17-34	18
β-strand	40-51	12	19
α-helix	56-58	3
β-strand	62	1	20
β-strand	63-78	16	19
β-strand	84-89	6	19
β-strand	97-100	4	19
α-helix	101-102	2
α-helix	106-109	4
α-helix	117-135	19
α-helix	137-140	4
α-helix	144-146	3
β-strand	147-154	8	19
α-helix	156-157	2
α-helix	162-179	18
β-strand	186	1	18
α-helix	187-194	8
α-helix	197-201	5
α-helix	208-215	8
β-strand	217	1	21
β-strand	220	1	21
β-strand	221-225	5	20
β-strand	231-235	5	20
α-helix	236-240	5
β-strand	244-251	8	22
α-helix	258-261	4
α-helix	266-283	18
β-strand	286	1	16
α-helix	302-313	12
α-helix	317-320	4
α-helix	324-342	19
β-strand	349	1	23
α-helix	351-357	7
α-helix	362-369	8
β-strand	375-377	3	2
β-strand	380	1	23
α-helix	382-404	23
α-helix	411-431	21
α-helix	438-448	11
β-strand	454-457	4	22
β-strand	465-472	8	22
α-helix	478-485	8
α-helix	486-490	5
α-helix	491-493	3
α-helix	499-505	7
β-strand	506-508	3	22
β-strand	516-519	4	19

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Galactose/lactose metabolism regulatory protein GAL80	A, B	protein	438	Saccharomyces cerevisiae	P04387 (AlphaFold model)
Protein GAL3	C, D	protein	520	Saccharomyces cerevisiae	P13045 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3V2U_1 Galactose/lactose metabolism regulatory protein GAL80 (chains A, B)
GSHMDYNKRSSVSTVPNAAPIRVGFVGLNAAKGWAIKTHYPAILQLSSQFQITALYSPKI
ETSIATIQRLKLSNATAFPTLESFASSSTIDMIVIAIQVASHYEVVMPLLEFSKNNPNLK
YLFVEWALACSLDQAESIYKAAAERGVQTIISLQGRKSPYILRAKELISQGYIGDINSIE
IAGNGGWYGYERPVKSPKYIYEIGNGVDLVTTTFGHTIDILQYMTSSYFSRINAMVFNNI
PEQELIDERGNRLGQRVPKTVPDHLLFQGTLLNGNVPVSCSFKGGKPTKKFTKNLVIDIH
GTKGDLKLEGDAGFAEISNLVLYYSGTRANDFPLANGQQAPLDPGYDAGKEIMEVYHLRN
YNAIVGNIHRLYQSISDFHFNTKKIPELPSQFVMQGFDFEGFPTLMDALILHRLIESVYK
SNMMGSTLNVSNISHYSL

Sequence of entity 2 (C, D), FASTA

>3V2U_2 Protein GAL3 (chains C, D)
SNTNVPIFSSPVRDLPRSFEQKHLAVVDAFFQTYHVKPDFIARSPGRVNLIGEHIDYCDF
SVLPLAIDVDMLCAVKILDEKNPSITLTNADPKFAQRKFDLPLDGSYMAIDPSVSEWSNY
FKCGLHVAHSYLKKIAPERFNNTPLVGAQIFCQSDIPTGGGLSSAFTCAAALATIRANMG
KNFDISKKDLTRITAVAEHYVGVNNGGMDQATSVYGEEDHALYVEFRPKLKATPFKFPQL
KNHEISFVIANTLVKSNKFETAPTNYNLRVIEVTVAANALATRYSVALPSHKDNSNSERG
NLRDFMDAYYARYENQAQPWNGDIGTGIERLLKMLQLVEESFSRKKSGFTVHEASTALNC
SREEFTRDYLTTFPVRFQVLKLYQRAKHVYSESLRVLKALKMMTSATFHTDEDFFTDFGR
LMNESQASCDKLYECSCIETNQICSIALANGSFGSRLTGAGWGGCTIHLVPSGANGNVEQ
VRKALIEKFYNVRYPDLTDEELKDAIIVSKPALGTCLYEQ

Ligands and cofactors

ID	Name	Formula	Copies
ATP	Adenosine-5'-triphosphate	C10 H16 N5 O13 P3	2
GLA	alpha-D-galactopyranose	C6 H12 O6	2
MG	Magnesium ion	Mg	2

Water and common crystallization additives (GOL) are not listed.

Primary citation

The Gal3p transducer of the GAL regulon interacts with the Gal80p repressor in its ligand-induced closed conformation. Lavy, T., Kumar, P.R., He, H. et al. Genes Dev (2012) 26:294-303. DOI 10.1101/gad.182691.111 · 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;…
3BTS 2.7 Å, Crystal structure of a ternary complex of the transcriptional repressor Gal80p (Gal80S0…
3BTU 2.85 Å, Crystal structure of the super-repressor mutant of Gal80p from Saccharomyces cerevisiae;…

Browse structure collections

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