Research workbench

T36-5 TCR specific for HLA-A24-NEF134-10

Analyse T36-5 TCR specific for HLA-A24-NEF134-10 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3VXT
Type: protein
Length: 880 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: T36-5 TCR alpha chain; T36-5 TCR beta chain
Pockets: 7 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C, A	T36-5 TCR alpha chain	protein	199	3% helix, 46% strand	—
D, B	T36-5 TCR beta chain	protein	241	7% helix, 51% strand	—

Pockets

7 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	996	0.77	0.79	108	empty
2	1103	0.72	0.75	102	empty
3	1029	0.71	0.75	94	empty
4	59	0.28	0.73	16	empty
5	51	0.28	0.75	12	empty

Interfaces

3 interfaces between chains.

C–D · 2230 Å² buried · 20 hydrogen bonds · protein-protein
A–B · 2225 Å² buried · 24 hydrogen bonds · protein-protein
C–A · 908 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

3VXT · T36-5 TCR specific for HLA-A24-Nef134-10 · the same entry in another collection · chain C against C, 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 3VXT · PDBe 3VXT

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