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C-SH2 domain of shp-2 in complex with phospho-itsm of pd-1

Analyse C-SH2 domain of shp-2 in complex with phospho-itsm of pd-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6R5G
Type
protein
Length
130 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tyrosine-protein phosphatase non-receptor type 11; Itsm
EC
3.1.3.48
UniProt
Q06124

Structure

solution nmr · 2 distinct chains · 16% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATyrosine-protein phosphatase non-receptor type 11 (EC 3.1.3.48)protein11918% helix, 29% strandQ06124
BItsmprotein110% helix, 0% strand—

Interfaces

1 interface between chains.

  • A–B · 739 Ų buried · 28 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

  • 6R5G · C-SH2 domain of SHP-2 in complex with phospho-ITSM of PD-1 · the same entry in another collection · chain A against A, TM-score 1.00

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