3BZD: T cell receptor beta chain 8.2

Manipulating the coupled folding and binding process drives affinity maturation in a protein-protein complex. Determined by X-ray diffraction at 2.3 Å resolution. Released 12 May 2009.

Method: X-ray diffraction
Resolution: 2.3 Å
Organisms: Mus musculus, Staphylococcus aureus
Chains: 2
Atoms: 2,849
Mol. weight: 39.65 kDa
Released: 12 May 2009

Explore 3BZD in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3BZD contains 9 α-helices and 30 β-strands across 2 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.

Chain A: 1 helix, 11 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	1
β-strand	10-13	4	2
β-strand	19-25	7	1
β-strand	31-37	7	2
β-strand	43-51	9	2
β-strand	54-57	4	2
β-strand	66-71	6	1
β-strand	74-79	6	1
α-helix	84-86	3
β-strand	89-95	7	2
β-strand	100-108	3	2
β-strand	112-116	5	2

Chain B: 8 helices, 19 β-strands

Element	Residues	Length	Sheet
α-helix	4-6	3
α-helix	8-10	3
α-helix	14-16	3
α-helix	22-25	4
β-strand	33-38	6	3
β-strand	42-43	2	4
β-strand	48-51	4	4
β-strand	61	1	5
β-strand	64-67	4	4
α-helix	71-78	8
β-strand	82-86	5	3
β-strand	89	1	4
β-strand	105	1	5
β-strand	108-110	3	4
β-strand	113-115	3	3
β-strand	127-135	9	6
β-strand	139-147	9	6
β-strand	152-153	2	7
α-helix	154-169	16
β-strand	173	1	8
β-strand	176	1	8
β-strand	179-188	10	6
β-strand	192-197	6	6
α-helix	208-212	5
α-helix	213-215	3
β-strand	220-221	2	7
β-strand	227-234	8	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
T cell receptor beta chain 8.2	A	protein	109	Mus musculus
Enterotoxin type C-3	B	protein	237	Staphylococcus aureus	P0A0L5 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3BZD_1 T cell receptor beta chain 8.2 (chains A)
AAVTQSPRNKVAVTGEKVTLSCQQTNNHNNMYWYRQDTGHGLRLIHYSYGAGSTEKGDIP
DGYKASRPSQEQFSLILESATPSQTSVYFCASGGGGTLYFGAGTRLSVL

Sequence of entity 2 (B), FASTA

>3BZD_2 Enterotoxin type C-3 (chains B)
ESQPDPMPDDLHKSSEFTGTMGNMKYLYDDHYVSATKVKSVDKFLAHDLIYNISDKKLKN
YDKVKTELLNEDLAKKYKDEVVDVYGSNYYVNCYFSSKDNVWWHGKTCMYGGITKHEGNH
FDNGNLQNVLVRVYENKRNTISFEVQTDKKSVTAQELDIKARNFLINKKNLYEFNSSPYE
TGYIKFIENNGNTFWYDMMPAPGDKFDQSKYLMMYNDNKTVDSKSVKIEVHLTTKNG

Primary citation

Manipulating the coupled folding and binding process drives affinity maturation in a protein-protein complex. Cho, S., Swaminathan, C.P., Kerzic, M.C. et al. To be published.

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…

Browse structure collections

About this viewer

MolViewer shows 3BZD directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.