MolNFT v1 · #181138 · protein

Inhibitory immune receptor protein complex

7LLJ · T cell receptor gamma variable 8: “Inhibitory immune receptor protein complex”. X-ray diffraction, 1 ligand (30W), 20 pockets (best druggability 0.76). MolNFT v1 #181138 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7LLJ
Type: protein
Length: 1,618 residues
Chains: 8
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: T cell receptor gamma variable 8; T cell receptor delta variable 3; Major…
UniProt: Q95460, P61769
Ligands: 30W
Pockets: 20 · best druggability 0.76

Structure

x-ray diffraction · 7 distinct chains · 13% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
K	T cell receptor gamma variable 8	protein	236	6% helix, 47% strand	—
L	T cell receptor delta variable 3	protein	211	4% helix, 43% strand	—
C	Major histocompatibility complex class I-related gene protein	protein	263	28% helix, 37% strand	Q95460
D, F	Beta-2-microglobulin	protein	97	0% helix, 40% strand	P61769
A	T cell receptor gamma variable 8	protein	237	6% helix, 48% strand	—
B	T cell receptor delta variable 3	protein	212	3% helix, 43% strand	—
E	Major histocompatibility complex class I-related gene protein	protein	265	28% helix, 36% strand	Q95460

Ligands and binding sites

30W · N-(6-formyl-4-oxo-3,4-dihydropteridin-2-yl)acetamide · ligand · 2 copies · chains C, E

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1141	0.76	0.79	83	empty
2	1006	0.75	0.78	84	empty
3	780	0.73	0.78	79	30W
4	658	0.72	0.79	76	30W
5	755	0.71	0.77	75	empty

Interfaces

11 interfaces between chains.

K–L · 2539 Å² buried · 24 hydrogen bonds · protein-protein
A–B · 2440 Å² buried · 22 hydrogen bonds · protein-protein
E–F · 1226 Å² buried · 10 hydrogen bonds · protein-protein
C–D · 1224 Å² buried · 16 hydrogen bonds · protein-protein
B–E · 738 Å² buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 16 disulfide, 2 covalent (disulfide, covalent ligand).

Compared structures

7LLJ · Inhibitory immune receptor protein complex · the same entry in another collection · chain F against F, TM-score 1.00
P61769 · AlphaFold monomer V2.0 prediction for beta-2-microglobulin (P61769) · a predicted model of the same protein · chain D against A, TM-score 0.97
Q95460 · AlphaFold monomer V2.0 prediction for major histocompatibility complex class I-related… · a predicted model of the same protein · chain C against A, TM-score 0.94

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 Q95460
Every structure of UniProt P61769
Elsewhere: RCSB PDB 7LLJ · PDBe 7LLJ · UniProt Q95460 · UniProt P61769

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.