J809.B5 TCR bound to IAb/3K. Determined by X-ray diffraction at 2.25 Å resolution. Released 28 May 2014.
Explore 4P23 in 3D Show helices and sheets RCSB PDB PDBe
4P23 contains 28 α-helices and 73 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-6 | 4 | 1 |
| β-strand | 9-13 | 5 | 2 |
| α-helix | 17 | 1 | |
| β-strand | 18-24 | 7 | 1 |
| β-strand | 31-37 | 7 | 2 |
| β-strand | 44-50 | 7 | 2 |
| β-strand | 56-59 | 4 | 1 |
| β-strand | 62-67 | 6 | 1 |
| β-strand | 72-77 | 6 | 1 |
| α-helix | 82-84 | 3 | |
| β-strand | 86-90 | 5 | 2 |
| β-strand | 91-92 | 2 | 3 |
| β-strand | 93 | 1 | 2 |
| β-strand | 100-101 | 2 | 3 |
| β-strand | 105-110 | 6 | 2 |
| α-helix | 111-112 | 2 | |
| β-strand | 119-125 | 7 | 4 |
| β-strand | 132-137 | 6 | 4 |
| α-helix | 146-148 | 3 | |
| β-strand | 153-155 | 3 | 4 |
| α-helix | 156-158 | 3 | |
| β-strand | 159-163 | 5 | 4 |
| α-helix | 164-166 | 3 | |
| β-strand | 168-177 | 10 | 4 |
| α-helix | 184-186 | 3 | |
| β-strand | 198 | 1 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-5 | 4 | 5 |
| β-strand | 8-12 | 5 | 6 |
| β-strand | 17-23 | 7 | 5 |
| β-strand | 29-36 | 8 | 6 |
| β-strand | 40-49 | 10 | 6 |
| β-strand | 52-55 | 4 | 6 |
| β-strand | 63-65 | 3 | 5 |
| β-strand | 71-76 | 6 | 5 |
| α-helix | 81-83 | 3 | |
| β-strand | 85-92 | 8 | 6 |
| β-strand | 100-101 | 2 | 6 |
| β-strand | 105-110 | 6 | 6 |
| α-helix | 113-115 | 3 | |
| β-strand | 117 | 1 | 7 |
| α-helix | 118-119 | 2 | |
| β-strand | 120-125 | 6 | 4 |
| α-helix | 126-127 | 2 | |
| α-helix | 128-134 | 7 | |
| β-strand | 136-146 | 11 | 4 |
| β-strand | 147 | 1 | 7 |
| β-strand | 151-157 | 7 | 8 |
| β-strand | 160-162 | 3 | 8 |
| β-strand | 166-168 | 3 | 4 |
| β-strand | 173-174 | 2 | 4 |
| β-strand | 184-193 | 10 | 4 |
| α-helix | 194-198 | 5 | |
| β-strand | 203-210 | 8 | 8 |
| β-strand | 213 | 1 | 9 |
| α-helix | 224-225 | 2 | |
| β-strand | 227 | 1 | 9 |
| β-strand | 229-236 | 8 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-15 | 12 | 10 |
| β-strand | 19-26 | 8 | 10 |
| β-strand | 29-35 | 7 | 10 |
| β-strand | 40-43 | 4 | 10 |
| α-helix | 46-51 | 6 | |
| β-strand | 53 | 1 | 11 |
| α-helix | 56-76 | 21 | |
| α-helix | 80-84 | 5 | |
| β-strand | 88-93 | 6 | 12 |
| β-strand | 103-112 | 10 | 12 |
| β-strand | 118-123 | 6 | 13 |
| β-strand | 126-128 | 3 | 13 |
| β-strand | 133-134 | 2 | 12 |
| α-helix | 137 | 1 | |
| β-strand | 138-139 | 2 | 12 |
| β-strand | 145-153 | 9 | 12 |
| β-strand | 161-166 | 6 | 13 |
| β-strand | 174-177 | 4 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | -24 | 1 | 11 |
| α-helix | -18--14 | 5 | |
| β-strand | 7-18 | 12 | 10 |
| β-strand | 23-32 | 10 | 10 |
| β-strand | 35-41 | 7 | 10 |
| β-strand | 46-49 | 4 | 10 |
| α-helix | 52-54 | 3 | |
| α-helix | 55-63 | 9 | |
| α-helix | 65-74 | 10 | |
| α-helix | 75-80 | 6 | |
| α-helix | 81-82 | 2 | |
| α-helix | 83-87 | 5 | |
| α-helix | 91-93 | 3 | |
| β-strand | 96 | 1 | 14 |
| α-helix | 97-98 | 2 | |
| β-strand | 99-104 | 6 | 15 |
| β-strand | 114-123 | 10 | 15 |
| β-strand | 124 | 1 | 14 |
| β-strand | 129-134 | 6 | 16 |
| β-strand | 137-139 | 3 | 16 |
| β-strand | 143-145 | 3 | 15 |
| α-helix | 146-148 | 3 | |
| β-strand | 149-150 | 2 | 15 |
| β-strand | 156-164 | 9 | 15 |
| β-strand | 171-177 | 7 | 16 |
| β-strand | 185-190 | 6 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| J809.B5 TCR V alpha chain (Va2.8) | A | protein | 199 | Mus musculus | |
| J809.B5 TCR V beta chain (Vb8.2) | B | protein | 239 | Mus musculus | |
| H-2 class II histocompatibility antigen, A-B alpha chain | C | protein | 179 | Mus musculus | P14434 (AlphaFold model) |
| 3K peptide and MHC IAb beta chain,H-2 class II histocompatibility antigen, A beta chain | D | protein | 218 | Mus musculus | P14483 (AlphaFold model) |
>4P23_1 J809.B5 TCR V alpha chain (Va2.8) (chains A) QVRQSPQSLTVWEGETAILNCSYENSAFDYFPWYQQFPGEGPALLIAIRSVSDKKEDGRF TIFFNKREKKLSLHITDSQPGDSATYFCAASKGADRLTFGKGTQLIIQPYIQNPDPAVYQ LRDSKSSDKSVCLFTDFDSETNVSESKDSDVYITDKCVLDMRSMDFKSNSAVAWSNKAAF ACANAFNNSIIPEDTFFPS
>4P23_2 J809.B5 TCR V beta chain (Vb8.2) (chains B) AVTQSPRNKVAVTGGKVTLSCDQTNNHNNMYWYRQDTGHGLRLIHYSYGAGSTEKGDIPD GYKASRPSQEDFSLILELATPSQTSVYFCASGDFWGDTLYFGAGTRLSVLEDLKNVFPPE VAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVCTDPQPLKEQPALN DSRYALSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGRA
>4P23_3 H-2 class II histocompatibility antigen, A-B alpha chain (chains C) IEADHVGTYGISVYQSPGDIGQYTFEFDGDELFYVDLDKKETVWMLPEFGQLASFDPQGG LQNIAVVKHNLGVLTKRSNSTPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPVINI TWLRNSKSVADGVYETSFFVNRDYSFHKLSYLTFIPSDDDIYDCKVEHWGLEEPVLKHW
>4P23_4 3K peptide and MHC IAb beta chain,H-2 class II histocompatibility antigen, A beta chain (chains D) FEAQKAKANKAVDGGGGSLVPRGSGGGGSERHFVYQFMGECYFTDGTQRIRYVTRYIYNR EEYVRYDSDVGEHRAVTELGRPDAEYWNSQPEILERTRAELDTVCRHNYEGPETHTSLRR LEQPNVVISLSRTEALNHHNTLVCSVTDFYPAKIKVRWFRNGQEETVGVSSTQLIRNGDW TFQVLVMLEMTPRRGEVYTCHVEHPSLKSPITVEWRAQ
Effect of CDR3 Sequences and Distal V Gene Residues in Regulating TCR-MHC Contacts and Ligand Specificity. Stadinski, B.D., Trenh, P., Duke, B. et al. J Immunol (2014) 192:6071-6082. DOI 10.4049/jimmunol.1303209 · PubMed
Other PDB entries of the same protein (UniProt P14434 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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