5KHQ: Rasip1 RA domain

Rasip1 RA domain. Determined by X-ray diffraction at 2.8 Å resolution. Released 19 Oct 2016.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Homo sapiens
Chains: 2
Atoms: 1,573
Mol. weight: 32.78 kDa
Released: 19 Oct 2016

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

Secondary structure: helices and β-sheets

5KHQ contains 11 α-helices and 12 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: 6 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	146-152	7	1
β-strand	161-166	6	1
α-helix	172-182	11
α-helix	199-201	3
β-strand	202-209	8	1
β-strand	225-228	4	1
α-helix	229-230	2
α-helix	235-241	7
β-strand	242-244	3	2
α-helix	245	1
β-strand	249-256	8	1
α-helix	257-263	7

Chain B: 5 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	146-152	7	3
β-strand	161-166	6	3
α-helix	172-181	10
β-strand	202-209	8	3
β-strand	223-228	6	3
α-helix	229-230	2
α-helix	235-241	7
β-strand	242-244	3	2
α-helix	245	1
β-strand	249-256	8	3
α-helix	257-263	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ras-interacting protein 1	A, B	protein	156	Homo sapiens	Q5U651 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5KHQ_1 Ras-interacting protein 1 (chains A, B)
GAMGEPPLATRATAPPGVLKIFGAGLASGANYKSVLATARSTARELVAEALERYGLAGSP
GGGPGESSCVDAFALCDALGRPAAAGVGSGEWRAEHLRVLGDSERPLLVQELWRARPGWA
RRFELRGREEARRLEQEAFGAADSEGTGAPSWRPQK

Primary citation

Structural Basis of Dimeric Rasip1 RA Domain Recognition of the Ras Subfamily of GTP-Binding Proteins. Gingras, A.R., Puzon-McLaughlin, W., Bobkov, A.A. et al. Structure (2016) 24:2152-2162. DOI 10.1016/j.str.2016.10.001 · PubMed

Other PDB entries of the same protein (UniProt Q5U651 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5KHO 2.78 Å, Rasip1 RA domain in complex with Rap1B

Browse structure collections

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