MolNFT v1 · #21463 · protein

T-cell receptor beta chain complexed with superantigen seb

1SBB · Protein (14.3.D T cell antigen receptor): “T-cell receptor beta chain complexed with superantigen seb”. X-ray diffraction, 9 pockets (best druggability 0.78). MolNFT v1 #21463 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 1SBB
Type: protein
Length: 950 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (14.3.D T cell antigen receptor); Protein (staphylococcal enterotoxin B)
UniProt: P01552
Pockets: 9 · best druggability 0.78

Structure

x-ray diffraction · 3 distinct chains · 14% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Protein (14.3.D T cell antigen receptor)	protein	238	5% helix, 47% strand	—
B	Protein (staphylococcal enterotoxin B)	protein	239	18% helix, 37% strand	P01552
D	Protein (staphylococcal enterotoxin B)	protein	235	19% helix, 37% strand	P01552

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	667	0.78	0.83	72	empty
2	303	0.63	0.80	43	empty
3	369	0.60	0.77	43	empty
4	442	0.59	0.75	52	empty
5	196	0.57	0.80	36	empty

Interfaces

5 interfaces between chains.

A–C · 616 Å² buried · 6 hydrogen bonds · protein-protein
C–D · 580 Å² buried · 4 hydrogen bonds · protein-protein
A–B · 572 Å² buried · 3 hydrogen bonds · protein-protein
B–C · 475 Å² buried · 2 hydrogen bonds · protein-protein
A–D · 338 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

1SBB · T-cell receptor beta chain complexed with superantigen seb · the same entry in another collection · chain A against A, TM-score 1.00
P01552 · AlphaFold monomer V2.0 prediction for enterotoxin type B (P01552) · a predicted model of the same protein · chain D against A, TM-score 0.97

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 P01552
Elsewhere: RCSB PDB 1SBB · PDBe 1SBB · UniProt P01552

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