3V00: PDB entry 3V00

Studies of a constitutively active G-alpha subunit provide insights into the mechanism of G protein activation. Determined by X-ray diffraction at 2.9 Å resolution. Released 18 Apr 2012.

Method: X-ray diffraction
Resolution: 2.9 Å
Organisms: Bos taurus, Rattus norvegicus
Chains: 3
Atoms: 8,788
Mol. weight: 124.33 kDa
Ligands: GDP
Released: 18 Apr 2012

Explore 3V00 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3V00 contains 58 α-helices and 22 β-strands across 3 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: 21 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	11-23	13
α-helix	26-28	3
β-strand	29-36	8	5
α-helix	42-53	12
α-helix	59-63	5
α-helix	66-84	19
α-helix	94-96	3
α-helix	99-109	11
α-helix	117-126	10
α-helix	130-137	8
α-helix	139-141	3
α-helix	147-151	5
α-helix	155-159	5
α-helix	167-171	5
β-strand	180-187	8	5
β-strand	190-197	8	5
α-helix	208-210	3
β-strand	214-222	9	5
α-helix	223-225	3
α-helix	238-251	14
α-helix	253-255	3
β-strand	259-265	7	5
α-helix	267-276	10
α-helix	279-281	3
α-helix	292-304	13
β-strand	316-320	5	5
α-helix	325-342	18

Chain B: 16 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	30-36	7	2
α-helix	42-52	11
α-helix	59-63	5
α-helix	66-86	21
α-helix	94-109	16
α-helix	117-126	10
α-helix	130-136	7
α-helix	148-153	6
α-helix	155-159	5
α-helix	167-171	5
β-strand	180-187	8	2
β-strand	190-197	8	2
β-strand	201	1	3
β-strand	203	1	3
α-helix	206-210	5
β-strand	214-222	9	2
α-helix	223-227	5
β-strand	229	1	4
β-strand	237	1	4
α-helix	238-251	14
β-strand	259-265	7	2
α-helix	267-273	7
α-helix	279-281	3
α-helix	292-304	13
β-strand	315-319	5	2
α-helix	325-341	17

Chain C: 21 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	19-22	4
β-strand	29-36	8	1
α-helix	42-53	12
α-helix	59-62	4
α-helix	66-86	21
α-helix	89-91	3
α-helix	96-109	14
α-helix	111	1
α-helix	117-128	12
α-helix	130-136	7
α-helix	139-141	3
α-helix	148-153	6
α-helix	155-159	5
α-helix	167-172	6
β-strand	180-186	7	1
β-strand	191-197	7	1
α-helix	207-210	4
β-strand	214-222	9	1
α-helix	223-225	3
α-helix	238-250	13
β-strand	259-265	7	1
α-helix	267-276	10
α-helix	279-281	3
α-helix	292-304	13
β-strand	315-319	5	1
α-helix	325-342	18
α-helix	344-347	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Guanine nucleotide-binding protein G(t) subunit alpha-1/ Guanine nucleotide-binding protein G(i)…	A, B, C	protein	356	Bos taurus, Rattus norvegicus	P04695 (AlphaFold model), P10824 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>3V00_1 Guanine nucleotide-binding protein G(t) subunit alpha-1/ Guanine nucleotide-binding protein G(i) subunit alpha-1 chimeric protein (chains A, B, C)
HHHHHHMGAGASAEEKHSRELEKKLKEDAEKDARTVKLLLLGAGESGKSTIVKQMKIIHQ
DPYSLEECLEFIAIIYGNTLQSILAIVRAMTTLNIQYGDSARQDDARKLMHMADTIEEGT
MPKEMSDIIQRLWKDSGIQACFDRASEYQLNDSAGYYLSDLERLVTPGYVPTEQDVLRSR
VKTTGIIETQFSFKDLNFRMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDE
EMNRMHESMHLFNSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEE
AGNYIKVQFLELNMRRDVKEIYSHMTCATDTQNVKFVFDAVTDIIIKENLKDCGLF

Ligands and cofactors

ID	Name	Formula	Copies
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	3

Primary citation

A constitutively active G-alpha subunit provide insights into the mechanism of G protein activation. Singh, G., Ramachandran, S., Cerione, R.A. Biochemistry (2012) 51:3232-3240. DOI 10.1021/bi3001984 · PubMed

Other PDB entries of the same protein (UniProt P04695 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1TAD 1.7 Å, Gtpase mechanism of gproteins from the 1.7-Å crystal structure of transducin…
1TAG 1.8 Å, Structural determinants for activation of the alpha-subunit of a heterotrimeric G protein
1GOT 2.0 Å, Heterotrimeric complex of a gt-alpha/gi-alpha chimera and the gt-beta-gamma subunits
1FQJ 2.02 Å, Crystal structure of the heterotrimeric complex of the rgs domain of RGS9, the gamma…
1TND 2.2 Å, The 2.2 Å crystal structure of transducin-alpha complexed with GTP gamma S
1FQK 2.3 Å, Crystal structure of the heterodimeric complex of the rgs domain of RGS9, and the GT/I1…
4J4Q 2.65 Å, Crystal structure of active conformation of GPCR opsin stabilized by octylglucoside
3PQR 2.85 Å, Crystal structure of Metarhodopsin II in complex with a C-terminal peptide derived from…
4BEY 2.9 Å, Night blindness causing G90D rhodopsin in complex with GaCT2 peptide
2X72 3.0 Å, Crystal structure of the constitutively active E113Q,D2C,D282C rhodopsin mutant with…
3DQB 3.2 Å, Crystal structure of the active G-protein-coupled receptor opsin in complex with a…
7JSN 3.2 Å, Structure of the Visual Signaling Complex between Transducin and Phosphodiesterase 6

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