1JCK: T-cell receptor beta chain

T-cell receptor beta chain complexed with SEC3 superantigen. Determined by X-ray diffraction at 3.5 Å resolution. Released 12 Nov 1997.

Method: X-ray diffraction
Resolution: 3.5 Å
Organisms: Mus musculus, Staphylococcus aureus
Chains: 4
Atoms: 7,540
Mol. weight: 108.47 kDa
Released: 12 Nov 1997

Explore 1JCK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1JCK contains 30 α-helices and 82 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chains A and C: 7 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	5-7	3	1
β-strand	10-14	5	2
β-strand	19-24	6	1
β-strand	31-37	7	2
β-strand	43-49	7	2
β-strand	56-57	2	2
β-strand	65-68	4	1
β-strand	74-79	6	1
α-helix	84-86	3
β-strand	88-95	8	2
α-helix	101-105	3
β-strand	106-108	3	2
β-strand	112-116A	6	2
α-helix	119-121	3
β-strand	123	1	3
α-helix	124-125	2
β-strand	126-130	5	4
α-helix	134-136	3
β-strand	145-152	8	4
β-strand	153	1	3
β-strand	157-163	7	5
β-strand	166-167	2	5
β-strand	172	1	4
β-strand	179-182	4	4
β-strand	189-196	8	4
α-helix	200-203	4
β-strand	209-216	8	5
α-helix	224-226	3
β-strand	236-242	7	5

Chains B and D: 8 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	4-7	4
α-helix	14-16	3
β-strand	17	1	6
α-helix	22-28	7
β-strand	33-38	6	7
β-strand	40-43	4	8
β-strand	48-52	5	8
β-strand	61-67	7	8
α-helix	71-77	7
β-strand	82-86	5	7
β-strand	89	1	8
β-strand	107-112	6	8
β-strand	115-117	3	7
β-strand	122	1	9
β-strand	131-137	7	10
β-strand	141-147	7	10
β-strand	151	1	9
β-strand	153-155	3	11
α-helix	156-170	15
β-strand	183-189	7	10
β-strand	195-199	5	10
α-helix	202-203	2
β-strand	205	1	6
α-helix	210-213	4
α-helix	214-217	4
β-strand	222-224	3	11
β-strand	229-235	7	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
14.3.D T cell antigen receptor	A, C	protein	238	Mus musculus
Staphylococcal enterotoxin C3	B, D	protein	239	Staphylococcus aureus	P0A0L5 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>1JCK_1 14.3.D T CELL ANTIGEN RECEPTOR (chains A, C)
AVTQSPRNKVAVTGGKVTLSCQQTNNHNNMYWYRQDTGHGLRLIHYSYGAGSTEKGDIPD
GYKASRPSQEQFSLILELATPSQTSVYFCASGGGRGSYAEQFFGPGTRLTVLEDLRQVTP
PKVSLFEPSKAEIANKQKATLVCLARGFFPDHVELSWWVNGKEVHSGVSTDPQAYKESNY
SYCLSSRLRVSATFWHNPRNHFRCQVQFHGLSEEDKWPEGSPKPVTQNISAEAWGRAD

Sequence of entity 2 (B, D), FASTA

>1JCK_2 STAPHYLOCOCCAL ENTEROTOXIN C3 (chains B, D)
ESQPDPMPDDLHKSSEFTGTMGNMKYLYDDHYVSATKVKSVDKFLAHDLIYNINDKKLNN
YDKVKTELLNEDLANKYKDEVVDVYGSNYYVNCYFSSKDNVGKVTSGKTCMYGGITKHEG
NHFDNGNLQNVLIRVYENKRNTISFEVQTDKKSVTAQELDIKARNFLINKKNLYEFNSSP
YETGYIKFIESNGNTFWYDMMPAPGDKFDQSKYLMIYKDNKMVDSKSVKIEVHLTTKNG

Primary citation

Crystal structure of a T-cell receptor beta-chain complexed with a superantigen. Fields, B.A., Malchiodi, E.L., Li, H. et al. Nature (1996) 384:188-192. DOI 10.1038/384188a0 · PubMed

Other PDB entries of the same protein (UniProt P0A0L5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2AQ2 1.8 Å, Crystal structure of T-cell receptor V beta domain variant complexed with superantigen…
1KLU 1.93 Å, Crystal structure of HLA-DR1/TPI(23-37) complexed with staphylococcal enterotoxin C3…
3BVG 2.0 Å, Manipulating the coupled folding and binding process drives affinity maturation in a…
3BVM 2.0 Å, Manipulating the coupled folding and binding process drives affinity maturation in a…
2AQ1 2.1 Å, Crystal structure of T-cell receptor V beta domain variant complexed with superantigen…
3BYY 2.2 Å, Manipulating the coupled folding and binding process drives affinity maturation in a…
1SJH 2.25 Å, HLA-DR1 complexed with a 13 residue HIV capsid peptide
1JWU 2.3 Å, Crystal Structure of the Complex of the MHC Class II Molecule HLA-DR1 (HA peptide…
2AQ3 2.3 Å, Crystal structure of T-cell receptor V beta domain variant complexed with superantigen…
2IPK 2.3 Å, Crystal Structure of the MHC Class II Molecule HLA-DR1 in Complex with the Fluorogenic…
3BVZ 2.3 Å, Manipulating the coupled folding and binding process drives affinity maturation in a…
3BYT 2.3 Å, A complex between a variant of staphylococcal enterotoxin C3 and the variable domain of…

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