MolNFT v1 · #43107 · protein

Structure of the DAP12-NKG2C transmembrane heterotrimer

2L35 · DAP12-NKG2C_TM: “Structure of the DAP12-NKG2C transmembrane heterotrimer”. Solution nmr, 1 pocket (best druggability 0.42). MolNFT v1 #43107 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2L35
Type: protein
Length: 95 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DAP12-NKG2C_TM; Tyro protein tyrosine kinase-binding protein
UniProt: O43914
Pockets: 1 · best druggability 0.42

Structure

solution nmr · 2 distinct chains · 75% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DAP12-NKG2C_TM	protein	63	71% helix, 0% strand	O43914
B	Tyro protein tyrosine kinase-binding protein	protein	32	81% helix, 0% strand	O43914

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	60	0.42	0.82	16	empty

Interfaces

1 interface between chains.

A–B · 1047 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

2L35 · Structure of the DAP12-NKG2C transmembrane heterotrimer · the same entry in another collection · chain A against A, TM-score 1.00
O43914 · AlphaFold monomer V2.0 prediction for tyro protein tyrosine kinase- binding protein… · a predicted model of the same protein · chain B against A, TM-score 0.69

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt O43914
Elsewhere: RCSB PDB 2L35 · PDBe 2L35 · UniProt O43914

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