5NP2: Abl1 SH3 pTyr89/134

Abl1 SH3 pTyr89/134. Determined by X-ray diffraction at 1.6 Å resolution. Released 16 May 2018.

Method
X-ray diffraction
Resolution
1.6 Å
Organism
Homo sapiens
Chains
2
Atoms
1,048
Mol. weight
13.82 kDa
Released
16 May 2018

Explore 5NP2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5NP2 contains 2 α-helices and 19 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: 1 helix, 10 β-strands

ElementResiduesLengthSheet
β-strand66-6831
β-strand7212
β-strand7613
β-strand7914
β-strand8212
β-strand87-8821
β-strand89-9354
β-strand99-10464
β-strand107-11264
α-helix113-1153
β-strand116-11831
Chain B: 1 helix, 9 β-strands
ElementResiduesLengthSheet
β-strand65-6845
β-strand7216
β-strand7613
β-strand7915
β-strand8216
β-strand87-9375
β-strand99-10465
β-strand107-11265
α-helix113-1153
β-strand116-11835

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Tyrosine-protein kinase ABL1A, Bprotein61Homo sapiensP00519 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>5NP2_1 Tyrosine-protein kinase ABL1 (chains A, B)
GSHMNLFVALYDFVASGDNTLSITKGEKLRVLGYNHNGEWCEAQTKNGQGWVPSNYITPV
N

Primary citation

Structural insights into the tyrosine phosphorylation-mediated inhibition of SH3 domain-ligand interactions. Mero, B., Radnai, L., Gogl, G. et al. J Biol Chem (2019) 294:4608-4620. DOI 10.1074/jbc.RA118.004732 · PubMed

Other PDB entries of the same protein (UniProt P00519 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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