1O4G: SH2

Crystal structure of SH2 in complex with DPI59. Determined by X-ray diffraction at 1.55 Å resolution. Released 17 Feb 2004.

Method
X-ray diffraction
Resolution
1.55 Å
Organism
Homo sapiens
Chains
1
Atoms
1,038
Mol. weight
12.63 kDa
Ligands
I59
Released
17 Feb 2004

Explore 1O4G in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1O4G contains 4 α-helices 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: 4 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand8-1031
α-helix14-218
α-helix26-272
β-strand31-3551
β-strand43-4971
β-strand57-6371
β-strand64-6522
β-strand71-7222
β-strand7912
α-helix82-898
β-strand10311
α-helix104-1052

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Proto-oncogene tyrosine-protein kinase srcAprotein108Homo sapiensP12931 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1O4G_1 PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC (chains A)
SIQAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKH
YKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGLCHRLTTVCPTSK

Ligands and cofactors

IDNameFormulaCopies
I59HYDROXY(1-naphthyl)methylphosphonic acidC11 H11 O4 P1

Primary citation

Requirements for specific binding of low affinity inhibitor fragments to the SH2 domain of (pp60)Src are identical to those for high affinity binding of full length inhibitors. Lange, G., Lesuisse, D., Deprez, P. et al. J Med Chem (2003) 46:5184-5195. DOI 10.1021/jm020970s · PubMed

Other PDB entries of the same protein (UniProt P12931 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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