5IH2: Adapter molecule crk

Structure, thermodynamics, and the role of conformational dynamics in the interactions between the N-terminal SH3 domain of CrkII and proline-rich motifs in cAbl. Determined by X-ray diffraction at 1.8 Å resolution. Released 29 Jun 2016.

Method: X-ray diffraction
Resolution: 1.8 Å
Organisms: Mus musculus, Endothia gyrosa
Chains: 4
Atoms: 1,388
Mol. weight: 17.04 kDa
Ligands: P4G
Released: 29 Jun 2016

Explore 5IH2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5IH2 contains 4 α-helices and 16 β-strands across 4 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: 1 helix, 8 β-strands

Element	Residues	Length	Sheet
β-strand	135-139	5	1
β-strand	143	1	2
β-strand	150	1	1
β-strand	153	1	2
β-strand	158-163	6	1
β-strand	169-173	5	1
β-strand	179-183	5	1
α-helix	184-186	3
β-strand	187-189	3	1

Chain B: 1 helix, 8 β-strands

Element	Residues	Length	Sheet
β-strand	136-139	4	3
β-strand	143	1	4
β-strand	150	1	3
β-strand	153	1	4
β-strand	158-163	6	3
β-strand	169-173	5	3
β-strand	179-183	5	3
α-helix	184-186	3
β-strand	187-188	2	3

Chain M: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	1-8	8

Chain N: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	2-8	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Adapter molecule crk	A, B	protein	58	Mus musculus	Q64010 (AlphaFold model)
Proline rich Peptide	M, N	protein	12	Endothia gyrosa	P00520 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>5IH2_1 Adapter molecule crk (chains A, B)
AEYVRALFDFNGNDEEDLPFKKGDILRIRDKPEEQWWNAEDSEGKRGMIPVPYVEKYR

Sequence of entity 2 (M, N), FASTA

>5IH2_2 Proline rich Peptide (chains M, N)
XYEKPALPRKRX

Ligands and cofactors

ID	Name	Formula	Copies
P4G	1-ethoxy-2-(2-ethoxyethoxy)ethane	C8 H18 O3	2

Water and common crystallization additives (NA, PEG) are not listed.

Primary citation

Binding Mechanism of the N-Terminal SH3 Domain of CrkII and Proline-Rich Motifs in cAbl. Bhatt, V.S., Zeng, D., Krieger, I. et al. Biophys J (2016) 110:2630-2641. DOI 10.1016/j.bpj.2016.05.008 · PubMed

Other PDB entries of the same protein (UniProt Q64010 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1CKA 1.5 Å, Structural basis for the specific interaction of lysine-containing proline-rich peptides…
5JN0 1.68 Å, CRK-II SH2 domain
5L23 1.77 Å, Crystal structure of the complex between the N-terminal SH3 domain of CrkII and a…
1CKB 1.9 Å, Structural basis for the specific interaction of lysine-containing proline-rich peptides…
1B07 2.5 Å, Crk SH3 domain complexed with peptoid inhibitor
1JU5 Ternary complex of an Crk SH2 domain, Crk-derived phophopeptide, and Abl SH3 domain by…
1M30 Solution structure of N-terminal SH3 domain from oncogene protein c-Crk
1M3A Solution structure of a circular form of the truncated N-terminal SH3 domain from…
1M3B Solution structure of a circular form of the N-terminal SH3 domain (A134C, E135G, R191G…
1M3C Solution structure of a circular form of the N-terminal SH3 domain (E132C, E133G, R191G…
2GGR Solution structure of the C-terminal SH3 domain of c-CrkII

Browse structure collections

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