Research workbench

H27-14 TCR specific for HLA-A24-NEF134-10

Analyse H27-14 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: 3VXQ
Type: protein
Length: 892 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: H27-14 TCR alpha chain; H27-14 TCR beta chain
Pockets: 11 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
D, A	H27-14 TCR alpha chain	protein	204	5% helix, 49% strand	—
E, B	H27-14 TCR beta chain	protein	242	7% helix, 49% strand	—

Pockets

11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	456	0.73	0.83	65	empty
2	926	0.72	0.76	78	empty
3	703	0.70	0.77	62	empty
4	96	0.54	0.84	19	empty
5	63	0.53	0.88	16	empty

Interfaces

5 interfaces between chains.

A–B · 2313 Å² buried · 25 hydrogen bonds · protein-protein
D–E · 2186 Å² buried · 26 hydrogen bonds · protein-protein
D–A · 583 Å² buried · 4 hydrogen bonds · protein-protein
D–B · 119 Å² buried · 1 hydrogen bond · protein-protein
E–B · 76 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

3VXQ · H27-14 TCR specific for HLA-A24-Nef134-10 · the same entry in another collection · chain D against D, 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 3VXQ · PDBe 3VXQ

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