2RMX: SHP-1 C-terminal SH2 domain

Solution structure of the SHP-1 C-terminal SH2 domain complexed with a tyrosine-phosphorylated peptide from NKG2A. Determined by solution NMR. Released 2 Dec 2008.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
1,008
Mol. weight
14.36 kDa
Released
2 Dec 2008

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

Secondary structure: helices and β-sheets

2RMX contains 2 α-helices and 10 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: 2 helices, 10 β-strands

ElementResiduesLengthSheet
β-strand9-1241
α-helix15-2511
β-strand30-3561
β-strand43-4861
β-strand62-6761
β-strand68-7032
β-strand73-7532
β-strand8212
α-helix85-9410
β-strand97-9933
β-strand103-10533
β-strand10911

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Tyrosine-protein phosphatase non-receptor type 6Aprotein118Homo sapiensP29350 (AlphaFold model)
NKG2-A/NKG2-B type II integral membrane proteinBprotein15P26715 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2RMX_1 Tyrosine-protein phosphatase non-receptor type 6 (chains A)
GSSGSSGWYHGHMSGGQAETLLQAKGEPWTFLVRESLSQPGDFVLSVLSDQPKAGPGSPL
RVTHIKVMCEGGRYTVGGLETFDSLTDLVEHFKKTGIEEASGAFVYLRQPYYSGPSSG
Sequence of entity 2 (B), FASTA
>2RMX_2 NKG2-A/NKG2-B type II integral membrane protein (chains B)
MDNQGVIYSDLNLPP

Primary citation

Structural basis for the recognition of the two NKG2A immunoreceptor tyrosine-based inhibitory motifs (ITIMs) by the C-terminal SH2 domain of protein tyrosine phosphatase SHP-1. Koshiba, S., Kasai, T., Sato, M. et al. To be published.

Other PDB entries of the same protein (UniProt P29350 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 2RMX directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.