2E3I: CLIP-170 CAP-Gly domain 1

Crystal structure of the CLIP-170 CAP-Gly domain 1. Determined by X-ray diffraction at 2.0 Å resolution. Released 28 Aug 2007.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
1
Atoms
667
Mol. weight
9.5 kDa
Released
28 Aug 2007

Explore 2E3I in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2E3I 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

ElementResiduesLengthSheet
β-strand63-6641
β-strand70-79101
β-strand86-9271
β-strand9911
β-strand102-10322
β-strand106-10722
β-strand116-11941
α-helix121-1233
β-strand124-12521

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
RestinAprotein86Homo sapiensP30622 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2E3I_1 Restin (chains A)
DDFRVGERVWVNGNKPGFIQFLGETQFAPGQWAGIVLDEPIGKNDGSVAGVRYFQCEPLK
GIFTRPSKLTRKVQAEDEANGLQTTP

Primary citation

Structural basis for tubulin recognition by cytoplasmic linker protein 170 and its autoinhibition. Mishima, M., Maesaki, R., Kasa, M. et al. Proc Natl Acad Sci U S A (2007) 104:10346-10351. DOI 10.1073/pnas.0703876104 · PubMed

Other PDB entries of the same protein (UniProt P30622 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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