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Crystal structure of the DM1 TCR at 2.75A

Analyse Crystal structure of the DM1 TCR at 2.75A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3DX9
Type: protein
Length: 884 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DM1 T cell receptor alpha chain; DM1 T cell receptor beta chain
Pockets: 7 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 46% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	DM1 T cell receptor alpha chain	protein	198	4% helix, 42% strand	—
B, D	DM1 T cell receptor beta chain	protein	244	7% helix, 49% strand	—

Pockets

7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	995	0.81	0.83	94	empty
2	1097	0.77	0.79	81	empty
3	97	0.38	0.76	19	empty
4	92	0.37	0.75	18	empty
5	84	0.36	0.76	17	empty

Interfaces

3 interfaces between chains.

C–D · 2396 Å² buried · 29 hydrogen bonds · protein-protein
A–B · 2389 Å² buried · 30 hydrogen bonds · protein-protein
A–D · 426 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

3DX9 · Crystal Structure of the DM1 TCR at 2.75A · 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 3DX9 · PDBe 3DX9

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