3T5G: Fully modified farnesylated Rheb

Structure of fully modified farnesylated Rheb in complex with PDE6D. Determined by X-ray diffraction at 1.7 Å resolution. Released 26 Oct 2011.

Method: X-ray diffraction
Resolution: 1.7 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,023
Mol. weight: 38.51 kDa
Ligands: GDP, MG, FAR
Released: 26 Oct 2011

Explore 3T5G in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3T5G contains 11 α-helices and 17 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: 5 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	4-13	10	1
α-helix	19-28	10
β-strand	41-49	9	1
β-strand	52-60	9	1
α-helix	72-74	3
β-strand	80-86	7	1
α-helix	90-106	17
β-strand	114-119	6	1
α-helix	131-140	10
β-strand	144-147	4	1
α-helix	153-168	16
β-strand	178	1	2

Chain B: 6 helices, 10 β-strands

Element	Residues	Length	Sheet
α-helix	5-14	10
β-strand	15-24	10	3
β-strand	30-34	5	3
β-strand	44-49	6	4
α-helix	51-55	5
β-strand	58-67	10	3
β-strand	71-82	12	4
β-strand	85-97	13	4
β-strand	101-110	10	3
β-strand	111	1	2
α-helix	112-113	2
α-helix	114-116	3
α-helix	118-119	2
α-helix	120-123	4
β-strand	127-135	9	4
β-strand	138-149	12	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
GTP-binding protein Rheb	A	protein	181	Homo sapiens	Q15382 (AlphaFold model)
Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta	B	protein	152	Homo sapiens	O43924 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3T5G_1 GTP-binding protein Rheb (chains A)
MPQSKSRKIAILGYRSVGKSSLTIQFVEGQFVDSYDPTIENTFTKLITVNGQEYHLQLVD
TAGQDEYSIFPQTYSIDINGYILVYSVTSIKSFEVIKVIHGKLLDMVGKVQIPIMLVGNK
KDLHMERVISYEEGKALAESWNAAFLESSAKENQTAVDVFRRIILEAEKMDGACSQGKSS
C

Sequence of entity 2 (B), FASTA

>3T5G_2 Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta (chains B)
GSMSAKDERAREILRGFKLNWMNLRDAETGKILWQGTEDLSVPGVEHEARVPKKILKCKA
VSRELNFSSTEQMEKFRLEQKVYFKGQCLEEWFFEFGFVIPNSTNTWQSLIEAAPESQMM
PASVLTGNVIIETKFFDDDLLVSTSRVRLFYV

Ligands and cofactors

ID	Name	Formula	Copies
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	1
MG	Magnesium ion	Mg	1
FAR	Farnesyl	C15 H26	1

Primary citation

Arl2-GTP and Arl3-GTP regulate a GDI-like transport system for farnesylated cargo. Ismail, S.A., Chen, Y.X., Rusinova, A. et al. Nat Chem Biol (2011) 7:942-949. DOI 10.1038/nchembio.686 · PubMed

Other PDB entries of the same protein (UniProt Q15382 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6BSX 1.65 Å, Crystal structure of rheb in complex with compound 1 at 1.65A resolution
1XTQ 2.0 Å, Structure of small GTPase human Rheb in complex with GDP
3SEA 2.0 Å, Structure of Rheb-Y35A mutant in GDP- and GMPPNP-bound forms
7BTD 2.0 Å, Crystal structure of Rheb Y35N mutant bound to GppNHp
5YXH 2.04 Å, Structure of Rheb-GDP
7BTC 2.1 Å, Crystal structure of Rheb Y35N mutant bound to GDP
6BT0 2.6 Å, Crystal structure of rheb in complex with compound NR1
7BTA 2.6 Å, Crystal structure of Rheb D60K mutant bound to GDP
1XTR 2.65 Å, Structure of small GTPase human Rheb in complex with GppNHp
1XTS 2.8 Å, Structure of small GTPase human Rheb in complex with GTP
9ED7 3.16 Å, Active state of mTOR on membrane
9ED4 3.23 Å, A composite map of mTORC1-Rag-Ragultor-4EBP1 on membrane

Browse structure collections

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