5C6R: PH domain of ASAP1

Crystal structure of PH domain of ASAP1. Determined by X-ray diffraction at 1.8 Å resolution. Released 7 Oct 2015.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Mus musculus
Chains: 2
Atoms: 1,838
Mol. weight: 35.15 kDa
Ligands: PO4
Released: 7 Oct 2015

Explore 5C6R in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5C6R contains 6 α-helices and 14 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.

Chains A and B: 3 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	342-349	8	1
β-strand	357-365	9	1
β-strand	368-371	4	1
α-helix	379-380	2
β-strand	381-384	4	1
α-helix	385-387	3
β-strand	389-392	4	1
β-strand	399-403	5	1
β-strand	408-412	5	1
α-helix	416-439	24

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Arf-GAP	A, B	protein	150	Mus musculus	Q9QWY8 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5C6R_1 Arf-GAP (chains A, B)
MGHHHHHHHHHHSSGHIDDDKHMGGYSMHQLQGNKEYGSEKKGFLLKKSDGIRKVWQRRK
CAVKNGILTISHATSNRQPAKLNLLTCQVKPNAEDKKSFDLISHNRTYHFQAEDEQDYIA
WISVLTNSKEEALTMAFRGEQSTGENSLED

Ligands and cofactors

ID	Name	Formula	Copies
PO4	Phosphate ion	O4 P	2

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

Primary citation

Molecular Basis for Cooperative Binding of Anionic Phospholipids to the PH Domain of the Arf GAP ASAP1. Jian, X., Tang, W.K., Zhai, P. et al. Structure (2015) 23:1977-1988. DOI 10.1016/j.str.2015.08.008 · PubMed

Other PDB entries of the same protein (UniProt Q9QWY8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8HLO 1.17 Å, Crystal structure of ASAP1-SH3 and MICAL1-PRM complex
5C79 1.6 Å, PH domain of ASAP1 in complex with diC4-PtdIns(4,5)P2
8ZE8 2.07 Å, Arf-GTPase activating protein Asap1 SH3 domain in complex with 440 Kd Ankyrin-B fragment

Browse structure collections

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