3V5R: Unliganded form of Gal3p

Crystal structure of the unliganded form of Gal3p. 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: 2
Atoms: 8,865
Mol. weight: 115.62 kDa
Released: 8 Feb 2012

Explore 3V5R in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3V5R contains 56 α-helices and 30 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: 28 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	20-34	15
β-strand	40-51	12	1
α-helix	56-58	3
β-strand	62	1	2
β-strand	63-77	15	1
β-strand	84-89	6	1
β-strand	97-100	4	1
α-helix	101-102	2
α-helix	106-109	4
α-helix	119-135	17
α-helix	137-140	4
α-helix	144-147	4
β-strand	148-154	7	1
α-helix	162-179	18
α-helix	187-195	9
α-helix	198-201	4
α-helix	208-215	8
β-strand	220-225	6	2
β-strand	231-236	6	2
α-helix	237-240	4
β-strand	244-251	8	3
α-helix	266-283	18
α-helix	289-291	3
α-helix	302-313	12
α-helix	317-320	4
α-helix	324-342	19
α-helix	343-345	3
β-strand	349	1	4
α-helix	351-357	7
α-helix	362-369	8
β-strand	380	1	4
α-helix	382-404	23
α-helix	411-427	17
α-helix	428-432	5
α-helix	438-449	12
β-strand	454-458	5	3
β-strand	465-472	8	3
α-helix	478-485	8
α-helix	486-490	5
α-helix	491-493	3
α-helix	499-505	7
β-strand	506-509	4	3
β-strand	516-519	4	1

Chain B: 28 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	22-34	13
β-strand	40-51	12	5
α-helix	56-58	3
β-strand	62	1	6
β-strand	63-78	16	5
β-strand	84-89	6	5
β-strand	97-100	4	5
α-helix	101-102	2
α-helix	106-108	3
α-helix	119-135	17
α-helix	137-140	4
α-helix	144-146	3
β-strand	147-154	8	5
α-helix	162-179	18
α-helix	187-195	9
α-helix	198-201	4
α-helix	208-215	8
β-strand	220-225	6	6
β-strand	231-236	6	6
α-helix	237-240	4
β-strand	244-251	8	7
α-helix	266-283	18
α-helix	287-291	5
α-helix	302-313	12
α-helix	319-320	2
α-helix	324-342	19
α-helix	343-345	3
β-strand	349	1	8
α-helix	351-357	7
α-helix	362-369	8
β-strand	380	1	8
α-helix	382-404	23
α-helix	411-427	17
α-helix	428-432	5
α-helix	438-448	11
β-strand	454-458	5	7
β-strand	465-472	8	7
α-helix	478-485	8
α-helix	486-490	5
α-helix	491-493	3
α-helix	499-504	6
β-strand	506-509	4	7
β-strand	516-519	4	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein GAL3	A, B	protein	505	Saccharomyces cerevisiae	P13045 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3V5R_1 Protein GAL3 (chains A, B)
SRSFEQKHLAVVDAFFQTYHVKPDFIARSPGRVNLIGEHIDYCDFSVLPLAIDVDMLCAV
KILDEKNPSITLTNADPKFAQRKFDLPLDGSYMAIDPSVSEWSNYFKCGLHVAHSYLKKI
APERFNNTPLVGAQIFCQSDIPTGGGLSSAFTCAAALATIRANMGKNFDISKKDLTRITA
VAEHYVGVNNGGMDQATSVYGEEDHALYVEFRPKLKATPFKFPQLKNHEISFVIANTLVK
SNKFETAPTNYNLRVIEVTVAANALATRYSVALPSHKDNSNSERGNLRDFMDAYYARYEN
QAQPWNGDIGTGIERLLKMLQLVEESFSRKKSGFTVHEASTALNCSREEFTRDYLTTFPV
RFQVLKLYQRAKHVYSESLRVLKALKMMTSATFHTDEDFFTDFGRLMNESQASCDKLYEC
SCIETNQICSIALANGSFGSRLTGAGWGGCTIHLVPSGANGNVEQVRKALIEKFYNVRYP
DLTDEELKDAIIVSKPALGTCLYEQ

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 P13045 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3V2U 2.1 Å, Crystal structure of the yeast GAL regulon complex of the repressor, Gal80p, and the…

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