2YDL: SH3C from CIN85

Crystal structure of SH3C from CIN85. Determined by X-ray diffraction at 2.05 Å resolution. Released 28 Mar 2012.

Method: X-ray diffraction
Resolution: 2.05 Å
Organism: HOMO SAPIENS
Chains: 1
Atoms: 603
Mol. weight: 8.03 kDa
Released: 28 Mar 2012

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

Secondary structure: helices and β-sheets

2YDL contains 1 α-helix and 8 β-strands across 1 chain. 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	270-274	5	1
β-strand	278	1	2
β-strand	285	1	1
β-strand	288	1	2
β-strand	293-298	6	1
β-strand	306-311	6	1
β-strand	314-319	6	1
α-helix	320-322	3
β-strand	323-325	3	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
SH3 domain-containing kinase-binding protein 1	A	protein	69	HOMO SAPIENS	Q96B97 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2YDL_1 SH3 DOMAIN-CONTAINING KINASE-BINDING PROTEIN 1 (chains A)
ASDYCKVIFPYEAQNDDELTIKEGDIVTLINKDCIDVGWWEGELNGRRGVFPDNFVKLLP
PLEHHHHHH

Primary citation

Distinct Ubiquitin Binding Modes Exhibited by SH3 Domains: Molecular Determinants and Functional Implications. Ortega Roldan, J.L., Casares, S., Ringkjobing Jensen, M. et al. PLoS One (2013) 8:73018. DOI 10.1371/JOURNAL.PONE.0073018 · PubMed

Other PDB entries of the same protein (UniProt Q96B97 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5ABS 1.74 Å, Crystal structure of the C-terminal coiled-coil domain of CIN85 in space group P321
2BZ8 2.0 Å, N-terminal Sh3 domain of CIN85 bound to Cbl-b peptide
2K6D CIN85 Sh3-C domain in complex with ubiquitin
2K9G Solution structure of the third SH3 domain of the Cin85 adapter protein
2N64 NMR Structure of the C-terminal Coiled-Coil Domain of CIN85
2O2O Solution structure of domain B from human CIN85 PROTEIN

Browse structure collections

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