9SOL: TCR-581
Structure of TCR-581 in complex with Peptide-HLA. Determined by X-ray diffraction at 2.93 Å resolution. Released 16 Sept 2026.
- Method
- X-ray diffraction
- Resolution
- 2.93 Å
- Organism
- Homo sapiens
- Chains
- 20
- Atoms
- 26,430
- Mol. weight
- 382.22 kDa
- Released
- 16 Sept 2026
Explore 9SOL in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9SOL contains 80 α-helices and 291 β-strands across 20 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: 9 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-12 | 10 | 1 |
| α-helix | 20 | 1 | |
| β-strand | 21-28 | 8 | 1 |
| β-strand | 31-37 | 7 | 1 |
| β-strand | 46-47 | 2 | 1 |
| α-helix | 50-52 | 3 | |
| α-helix | 57-84 | 28 | |
| β-strand | 94-103 | 10 | 1 |
| β-strand | 109-118 | 10 | 1 |
| β-strand | 121-126 | 6 | 1 |
| β-strand | 133-135 | 3 | 1 |
| α-helix | 138-149 | 12 | |
| α-helix | 152-161 | 10 | |
| α-helix | 163-174 | 12 | |
| α-helix | 176-179 | 4 | |
| β-strand | 183 | 1 | 2 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-192 | 7 | 3 |
| β-strand | 198-208 | 11 | 3 |
| β-strand | 209 | 1 | 2 |
| β-strand | 214-219 | 6 | 4 |
| β-strand | 222-224 | 3 | 4 |
| β-strand | 228-230 | 3 | 3 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 3 |
| β-strand | 241-250 | 10 | 3 |
| β-strand | 257-262 | 6 | 4 |
| β-strand | 270-273 | 4 | 4 |
Chains B and Q: 1 helix, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3 | 1 | 5 |
| α-helix | 4-5 | 2 | |
| β-strand | 6-11 | 6 | 6 |
| β-strand | 21-30 | 10 | 6 |
| β-strand | 31 | 1 | 5 |
| β-strand | 36-41 | 6 | 7 |
| β-strand | 44-46 | 3 | 7 |
| β-strand | 50-51 | 2 | 6 |
| β-strand | 55-56 | 2 | 6 |
| β-strand | 62-70 | 9 | 6 |
| β-strand | 78-83 | 6 | 7 |
| β-strand | 91-94 | 4 | 7 |
Chains C, H, M and R: 0 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5 | 1 | 8 |
Chain D: 2 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-6 | 2 | 9 |
| β-strand | 12-15 | 4 | 10 |
| β-strand | 20-26 | 7 | 9 |
| β-strand | 33-39 | 7 | 10 |
| β-strand | 45-51 | 7 | 10 |
| β-strand | 55-59 | 5 | 9 |
| β-strand | 62-67 | 6 | 9 |
| β-strand | 72-77 | 6 | 9 |
| α-helix | 82-84 | 3 | |
| β-strand | 86-93 | 8 | 10 |
| β-strand | 96 | 1 | 8 |
| β-strand | 99 | 1 | 8 |
| β-strand | 103-104 | 2 | 10 |
| β-strand | 108-113 | 6 | 10 |
| β-strand | 122-128 | 7 | 11 |
| β-strand | 135-140 | 6 | 11 |
| β-strand | 156-158 | 3 | 11 |
| β-strand | 162-166 | 5 | 11 |
| β-strand | 171-180 | 10 | 11 |
| α-helix | 187-190 | 4 | |
Chain E: 6 helices, 23 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-7 | 3 | 12 |
| β-strand | 10-14 | 5 | 13 |
| β-strand | 19-24 | 6 | 12 |
| β-strand | 31-37 | 7 | 13 |
| β-strand | 44-50 | 7 | 13 |
| β-strand | 53-56 | 4 | 13 |
| β-strand | 65-68 | 4 | 12 |
| β-strand | 75-79 | 5 | 12 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-95 | 8 | 13 |
| α-helix | 100-101 | 2 | |
| β-strand | 102-103 | 2 | 13 |
| β-strand | 107-112 | 6 | 13 |
| α-helix | 115-117 | 3 | |
| β-strand | 119 | 1 | 14 |
| β-strand | 125-127 | 3 | 11 |
| β-strand | 138-148 | 11 | 11 |
| β-strand | 149 | 1 | 14 |
| β-strand | 153-159 | 7 | 15 |
| β-strand | 168-170 | 3 | 11 |
| α-helix | 174 | 1 | |
| β-strand | 175-176 | 2 | 11 |
| β-strand | 186-195 | 10 | 11 |
| α-helix | 196-200 | 5 | |
| β-strand | 205-212 | 8 | 15 |
| β-strand | 215 | 1 | 16 |
| α-helix | 226-227 | 2 | |
| β-strand | 229 | 1 | 16 |
| β-strand | 231-238 | 8 | 15 |
Chains F and P: 10 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-12 | 10 | 17 |
| α-helix | 20 | 1 | |
| β-strand | 21-28 | 8 | 17 |
| β-strand | 31-37 | 7 | 17 |
| β-strand | 46-47 | 2 | 17 |
| α-helix | 51-54 | 4 | |
| α-helix | 57-84 | 28 | |
| β-strand | 94-103 | 10 | 17 |
| β-strand | 109-118 | 10 | 17 |
| β-strand | 121-126 | 6 | 17 |
| β-strand | 133-135 | 3 | 17 |
| α-helix | 138-149 | 12 | |
| α-helix | 152-161 | 10 | |
| α-helix | 163-174 | 12 | |
| α-helix | 176-179 | 4 | |
| β-strand | 183 | 1 | 18 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-193 | 8 | 19 |
| β-strand | 198-208 | 11 | 19 |
| β-strand | 209 | 1 | 18 |
| β-strand | 214-219 | 6 | 20 |
| β-strand | 222-224 | 3 | 20 |
| β-strand | 228-230 | 3 | 19 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 19 |
| β-strand | 241-250 | 10 | 19 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-262 | 6 | 20 |
| β-strand | 270-273 | 4 | 20 |
Chain G: 2 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3 | 1 | 21 |
| α-helix | 4-5 | 2 | |
| β-strand | 6-11 | 6 | 22 |
| β-strand | 21-30 | 10 | 22 |
| β-strand | 31 | 1 | 21 |
| β-strand | 36-41 | 6 | 23 |
| β-strand | 44-46 | 3 | 23 |
| β-strand | 50-51 | 2 | 22 |
| α-helix | 52-54 | 3 | |
| β-strand | 55-56 | 2 | 22 |
| β-strand | 62-70 | 9 | 22 |
| β-strand | 78-83 | 6 | 23 |
| β-strand | 91-94 | 4 | 23 |
Chains I and S: 1 helix, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-6 | 2 | 25 |
| β-strand | 12-15 | 4 | 26 |
| β-strand | 20-26 | 7 | 25 |
| β-strand | 33-39 | 7 | 26 |
| β-strand | 46-51 | 6 | 26 |
| β-strand | 55-59 | 5 | 25 |
| β-strand | 62-67 | 6 | 25 |
| β-strand | 72-77 | 6 | 25 |
| α-helix | 82-84 | 3 | |
| β-strand | 86-93 | 8 | 26 |
| β-strand | 96 | 1 | 24 |
| β-strand | 99 | 1 | 24 |
| β-strand | 103-104 | 2 | 26 |
| β-strand | 108-113 | 6 | 26 |
| β-strand | 122-128 | 7 | 27 |
| β-strand | 135-140 | 6 | 27 |
| β-strand | 156-158 | 3 | 27 |
| β-strand | 162-166 | 5 | 27 |
| β-strand | 171-180 | 10 | 27 |
6 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| MHC class I antigen | A, F, K, P | protein | 276 | Homo sapiens | A0A5B8RNS7 (AlphaFold model) |
| Beta-2-microglobulin | B, G, L, Q | protein | 100 | Homo sapiens | P61769 (AlphaFold model) |
| Piwi-like protein 1 | C, H, M, R | protein | 9 | Homo sapiens | Q96J94 (AlphaFold model) |
| TCR alpha | D, I, N, S | protein | 208 | Homo sapiens | |
| TCR beta | E, J, O, T | protein | 242 | Homo sapiens | |
Sequence of entity 1 (A, F, K, P), FASTA
>9SOL_1 MHC class I antigen (chains A, F, K, P)
GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYW
DGETRKVKAHSQTHRVDLGTLRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYDG
KDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAYLEGTCVEWLRRYLENGKETLQ
RTDAPKTHMTHHAVSDHEATLRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT
FQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEP
Sequence of entity 2 (B, G, L, Q), FASTA
>9SOL_2 Beta-2-microglobulin (chains B, G, L, Q)
MIQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKD
WSFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
Sequence of entity 3 (C, H, M, R), FASTA
>9SOL_3 Piwi-like protein 1 (chains C, H, M, R)
SLSNRLYYL
Sequence of entity 4 (D, I, N, S), FASTA
>9SOL_4 TCR alpha (chains D, I, N, S)
MAKEVEQNSGPLSVPEGAIASLNCTYSDRGSQSFFWYRQYSGKSPELIMSIYSNGDKEDG
RFTAQLNKASQYVSLLIRDSQPSDSATYLCAVNDSNFGNEKLTFGTGTRLTIIPNIQNPD
PAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLDMRSMDFKSNSAVAWS
NKSDFACANAFNNSIIPEDTFFPSPESS
Sequence of entity 5 (E, J, O, T), FASTA
>9SOL_5 TCR beta (chains E, J, O, T)
NAGVMQNPRHLVRRRGQEARLRCSPMKGHSHVYWYRQLPEEGLKFMVYLQKENIIDESGM
PKERFSAEFPKEGPSILRIQQVVRGDSAAYFCASSAGTTEQYFGPGTRLTVTEDLNKVFP
PEVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVCTDPQPLKEQPA
LNDSRYALSSRLRVSATFWQDPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGR
AD
Primary citation
Isolation of Human TCRs specific to any peptide-HLA complex. Karuppiah, V., Rangel, V.L. Nat Commun (2026).
Other PDB entries of the same protein (UniProt A0A5B8RNS7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 9GV7 1.86 Å, Structure of reverse docking TCR in complex with peptide-HLA
- 6TMO 2.1 Å, Structure determination of an enhanced affinity TCR, a24b17, in complex with HLA-A*02:01…
- 9DL1 2.3 Å, Crystal Structure of HLA-A*02:01/NY-ESO-1 (SLLMWITQV) and a target specific TRACeR-I
- 9SOK 2.5 Å, Structure of three-domain single chain TCR-581 in complex with Peptide-HLA
- 9GV6 2.77 Å, Structure of TCR in complex with peptide-HLA
Browse structure collections
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