2R09: Cytohesin-3

Crystal Structure of Autoinhibited Form of Grp1 Arf GTPase Exchange Factor. Determined by X-ray diffraction at 1.9 Å resolution. Released 4 Dec 2007.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Mus musculus
Chains: 2
Atoms: 6,538
Mol. weight: 83.9 kDa
Ligands: PE5, 4IP
Released: 4 Dec 2007

Explore 2R09 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2R09 contains 34 α-helices and 22 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: 18 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	60-62	3
α-helix	64-79	16
α-helix	81-90	10
α-helix	98-107	10
α-helix	113-121	9
α-helix	125-136	12
α-helix	145-152	8
α-helix	162-179	18
α-helix	187-205	19
α-helix	212-214	3
α-helix	215-221	7
β-strand	226	1	1
β-strand	229	1	1
α-helix	230-232	3
α-helix	233-245	13
α-helix	247-249	3
α-helix	258-260	3
β-strand	267-274	8	2
β-strand	281-289	9	2
β-strand	292-296	5	2
β-strand	306-309	4	2
β-strand	314-318	5	2
β-strand	326-330	5	2
α-helix	337-340	4
β-strand	342-344	3	2
β-strand	350-352	3	2
β-strand	358-361	4	2
α-helix	365-380	16
α-helix	383-395	13

Chain B: 16 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	61-79	19
α-helix	81-90	10
α-helix	98-107	10
α-helix	113-120	8
α-helix	125-136	12
α-helix	145-152	8
α-helix	162-179	18
α-helix	187-205	19
α-helix	215-221	7
β-strand	226	1	3
β-strand	229	1	3
α-helix	230-232	3
α-helix	233-245	13
α-helix	247-249	3
α-helix	258-260	3
β-strand	267-274	8	4
β-strand	281-289	9	4
β-strand	292-296	5	4
β-strand	306-309	4	4
β-strand	314-318	5	4
β-strand	326-330	5	4
α-helix	337-339	3
β-strand	342-344	3	4
β-strand	350-352	3	4
β-strand	357-361	5	4
α-helix	365-380	16
α-helix	382-393	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cytohesin-3	A, B	protein	347	Mus musculus	O08967 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2R09_1 Cytohesin-3 (chains A, B)
MGHHHHHHGSTTQRNAQIAMGRKKFNMDPKKGIQFLIENDLLQSSPEDVAQFLYKGEGLN
KTVIGDYLGERDDFNIKVLQAFVELHEFADLNLVQALRQFLWSFRLPGEAQKIDRMMEAF
ASRYCLCNPGVFQSTDTCYVLSFAIIMLNTSLHNHNVRDKPTAERFITMNRGINEGGDLP
EELLRNLYESIKNEPFKIPEDDGNDLTYTFFNPDREGWLLKLGGRVKTWKRRWFILTDNC
LYYFEYTTDKEPRGIIPLENLSIREVEDPRKPNCFELYNPSHKGQVIKACKTEADGRVVE
GNHVVYRISAPSPEEKEEWMKSIKASISRDPFYDMLATRKRRIANKK

Ligands and cofactors

ID	Name	Formula	Copies
PE5	3,6,9,12,15,18,21,24-octaoxahexacosan-1-ol	C18 H38 O9	1
4IP	Inositol-(1,3,4,5)-tetrakisphosphate	C6 H16 O18 P4	2

Water and common crystallization additives (PGE, SO4) are not listed.

Primary citation

Structural Basis and Mechanism of Autoregulation in 3-Phosphoinositide-Dependent Grp1 Family Arf GTPase Exchange Factors. DiNitto, J.P., Delprato, A., Gabe Lee, M.T. et al. Mol Cell (2007) 28:569-583. DOI 10.1016/j.molcel.2007.09.017 · PubMed

Other PDB entries of the same protein (UniProt O08967 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1FGY 1.5 Å, GRP1 PH domain with INS(1,3,4,5)P4
1U2B 1.8 Å, Triglycine variant of the Grp1 Pleckstrin Homology Domain unliganded
1FHW 1.9 Å, Structure of the pleckstrin homology domain from GRP1 in complex with…
2R0D 2.04 Å, Crystal Structure of Autoinhibited Form of Grp1 Arf GTPase Exchange Factor
1FGZ 2.05 Å, GRP1 PH domain (unliganded)
1FHX 2.5 Å, Structure of the pleckstrin homology domain from GRP1 in complex with inositol…
6BBP 35.0 Å, Model for compact volume of truncated monomeric Cytohesin-3 (Grp1; amino acids 63-399)…
6BBQ 35.0 Å, Model for extended volume of truncated monomeric Cytohesin-3 (Grp1; amino acids 63-399)…

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