2APT: T-cell receptor beta chain V

Crystal Structure of the G17E/S54N/K66E/Q72H/E80V/L81S/T87S/G96V variant of the murine T cell receptor V beta 8.2 domain. Determined by X-ray diffraction at 2.0 Å resolution. Released 21 Mar 2006.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Rattus norvegicus
Chains
2
Atoms
1,764
Mol. weight
24.42 kDa
Ligands
MLA
Released
21 Mar 2006

Explore 2APT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2APT contains 2 α-helices and 22 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

ElementResiduesLengthSheet
β-strand4-741
β-strand10-1342
β-strand19-2571
β-strand31-3882
β-strand42-4982
β-strand56-5722
β-strand65-6841
β-strand74-7961
α-helix84-863
β-strand88-9692
β-strand99-10842
β-strand112-11652
Chain B: 1 helix, 11 β-strands
ElementResiduesLengthSheet
β-strand4-743
β-strand10-1344
β-strand19-2573
β-strand31-3884
β-strand42-4984
β-strand56-5724
β-strand65-7173
β-strand74-7963
α-helix84-863
β-strand88-9584
β-strand101-10824
β-strand112-11654

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
T-cell receptor beta chain VA, Bprotein112Rattus norvegicusP04213 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>2APT_1 T-cell receptor beta chain V (chains A, B)
ILEAAVTQSPRNKVAVTGEKVTLSCQQTNNHNNMYWYRQDTGHGLRLIHYSYGAGNTEKG
DIPDGYEASRPSHEQFSLILVSATPSQSSVYFCASGVGGTLYFGAGTRLSVL

Ligands and cofactors

IDNameFormulaCopies
MLAMalonic acidC3 H4 O41

Primary citation

Structural basis of affinity maturation and intramolecular cooperativity in a protein-protein interaction. Cho, S., Swaminathan, C.P., Yang, J. et al. Structure (2005) 13:1775-1787. DOI 10.1016/j.str.2005.08.015 · PubMed

Other PDB entries of the same protein (UniProt P04213 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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