2PLE: Phospholipase C gamma-1, C-terminal SH2 domain

Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-GAMMA1 complexed with a high affinity binding peptide. Determined by solution NMR. Released 26 Jan 1995.

Method
Solution NMR
Organism
Bos taurus
Chains
2
Atoms
965
Mol. weight
13.76 kDa
Released
26 Jan 1995

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

Secondary structure: helices and β-sheets

2PLE contains 2 α-helices and 12 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: 2 helices, 11 β-strands

ElementResiduesLengthSheet
β-strand12-1321
α-helix20-267
β-strand33-3422
β-strand36-3831
β-strand45-4621
β-strand49-5022
β-strand5612
β-strand5813
β-strand59-6021
β-strand61-6224
β-strand67-6824
β-strand7314
α-helix77-8610
Chain B: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand513

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Phospholipase C gamma-1, C-terminal SH2 domainAprotein105Bos taurusP08487 (AlphaFold model)
Phosphopeptide from pdgfBprotein12Bos taurusP09619 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2PLE_1 PHOSPHOLIPASE C GAMMA-1, C-TERMINAL SH2 DOMAIN (chains A)
GSPGIHESKEWYHASLTRAQAEHMLMRVPRDGAFLVRKRNEPNSYAISFRAEGKIKHCRV
QQEGQTVMLGNSEFDSLVDLISYYEKHPLYRKMKLRYPINEENSS
Sequence of entity 2 (B), FASTA
>2PLE_2 PHOSPHOPEPTIDE FROM PDGF (chains B)
DNDYIIPLPDPK

Primary citation

Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide. Pascal, S.M., Singer, A.U., Gish, G. et al. Cell (1994) 77:461-472. DOI 10.1016/0092-8674(94)90160-0 · PubMed

Other PDB entries of the same protein (UniProt P08487 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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