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MHC-independent T cell receptor A11

Analyse MHC-independent T cell receptor A11 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6C68
Type: protein
Length: 886 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: T-cell receptor alpha chain; T-cell receptor beta chain
Pockets: 10 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	T-cell receptor alpha chain	protein	205	4% helix, 45% strand	—
B, D	T-cell receptor beta chain	protein	238	8% helix, 51% strand	—

Pockets

10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1186	0.75	0.77	102	empty
2	934	0.73	0.77	76	empty
3	867	0.72	0.77	80	empty
4	120	0.41	0.76	22	empty
5	110	0.38	0.75	21	empty

Interfaces

4 interfaces between chains.

A–B · 2297 Å² buried · 22 hydrogen bonds · protein-protein
C–D · 2210 Å² buried · 19 hydrogen bonds · protein-protein
B–D · 578 Å² buried · 7 hydrogen bonds · protein-protein
A–D · 187 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

6C68 · MHC-independent t cell receptor A11 · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 6C68 · PDBe 6C68

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