1FHX: Pleckstrin homology domain from GRP1

Structure of the pleckstrin homology domain from GRP1 in complex with inositol 1,3,4,5-tetrakisphosphate. Determined by X-ray diffraction at 2.5 Å resolution. Released 23 Aug 2000.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Mus musculus
Chains: 2
Atoms: 2,254
Mol. weight: 31.91 kDa
Ligands: 4IP
Released: 23 Aug 2000

Explore 1FHX in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1FHX contains 4 α-helices and 18 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: 2 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	267-274	8	1
β-strand	281-289	9	1
β-strand	292-296	5	1
β-strand	306-309	4	1
β-strand	314-317	4	1
β-strand	326-330	5	1
α-helix	332-334	3
β-strand	342-344	3	1
β-strand	350-352	3	1
β-strand	358-361	4	1
α-helix	365-380	16

Chain B: 2 helices, 9 β-strands

Element	Residues	Length	Sheet
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	357-361	5	2
α-helix	365-378	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Guanine nucleotide exchange factor and integrin binding protein homolog GRP1	A, B	protein	129	Mus musculus	O08967 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>1FHX_1 GUANINE NUCLEOTIDE EXCHANGE FACTOR AND INTEGRIN BINDING PROTEIN HOMOLOG GRP1 (chains A, B)
MNPDREGWLLKLGGRVKTWKRRWFILTDNCLYYFEYTTDKEPRGIIPLENLSIREVEDPR
KPNCFELYNPSHKGQVIKACKTEADGRVVEGNHVVYRISAPSPEEKEEWMKSIKASISRD
PFYDMLATR

Ligands and cofactors

ID	Name	Formula	Copies
4IP	Inositol-(1,3,4,5)-tetrakisphosphate	C6 H16 O18 P4	2

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

Primary citation

Structural basis for discrimination of 3-phosphoinositides by pleckstrin homology domains. Ferguson, K.M., Kavran, J.M., Sankaran, V.G. et al. Mol Cell (2000) 6:373-384. DOI 10.1016/S1097-2765(00)00037-X · 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…
2R09 1.9 Å, Crystal Structure of Autoinhibited Form of Grp1 Arf GTPase Exchange Factor
2R0D 2.04 Å, Crystal Structure of Autoinhibited Form of Grp1 Arf GTPase Exchange Factor
1FGZ 2.05 Å, GRP1 PH domain (unliganded)
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)…

Browse structure collections

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