2NX5: ELS4 TCR
Crystal structure of ELS4 TCR bound to HLA-B*3501 presenting EBV peptide EPLPQGQLTAY at 1.7A. Determined by X-ray diffraction at 2.7 Å resolution. Released 27 Feb 2007.
- Method
- X-ray diffraction
- Resolution
- 2.7 Å
- Organism
- Homo sapiens
- Chains
- 20
- Atoms
- 26,481
- Mol. weight
- 372.98 kDa
- Released
- 27 Feb 2007
Explore 2NX5 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2NX5 contains 98 α-helices and 286 β-strands across 19 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: 11 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-14 | 12 | 1 |
| β-strand | 18-28 | 11 | 1 |
| β-strand | 31-37 | 7 | 1 |
| β-strand | 46-47 | 2 | 1 |
| α-helix | 50-54 | 5 | |
| 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 | 152-158 | 7 | |
| α-helix | 159-163 | 5 | |
| α-helix | 164-174 | 11 | |
| α-helix | 176-179 | 4 | |
| α-helix | 182 | 1 | |
| β-strand | 183 | 1 | 2 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-193 | 8 | 3 |
| β-strand | 199-208 | 10 | 3 |
| β-strand | 209 | 1 | 2 |
| β-strand | 214-219 | 6 | 4 |
| β-strand | 222-223 | 2 | 4 |
| β-strand | 228-230 | 3 | 3 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 3 |
| β-strand | 241-249 | 9 | 3 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-262 | 6 | 4 |
| β-strand | 270-272 | 3 | 4 |
Chain B: 3 helices, 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 | 44-45 | 2 | 7 |
| α-helix | 46 | 1 | |
| β-strand | 50-51 | 2 | 6 |
| α-helix | 52-54 | 3 | |
| 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, M and S: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-4 | 3 | |
Chain D: 3 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-4 | 2 | 8 |
| β-strand | 9-13 | 5 | 9 |
| β-strand | 18-24 | 7 | 8 |
| β-strand | 29-37 | 9 | 9 |
| β-strand | 43-49 | 7 | 9 |
| β-strand | 53-57 | 5 | 8 |
| β-strand | 62-67 | 6 | 8 |
| β-strand | 72-77 | 6 | 8 |
| α-helix | 82-84 | 3 | |
| β-strand | 86-94 | 9 | 9 |
| β-strand | 105-106 | 2 | 9 |
| β-strand | 110-115 | 6 | 9 |
| α-helix | 116 | 1 | |
| β-strand | 124-128 | 5 | 10 |
| β-strand | 129-130 | 2 | 11 |
| β-strand | 138-142 | 5 | 10 |
| β-strand | 158-160 | 3 | 10 |
| α-helix | 161-163 | 3 | |
| β-strand | 164-168 | 5 | 10 |
| β-strand | 173-182 | 10 | 10 |
Chain E: 7 helices, 24 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 | 43-51 | 9 | 13 |
| β-strand | 54-57 | 4 | 13 |
| β-strand | 66-68 | 3 | 12 |
| β-strand | 74-79 | 6 | 12 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-95 | 8 | 13 |
| β-strand | 107-108 | 2 | 13 |
| β-strand | 112-117 | 6 | 13 |
| α-helix | 120-122 | 3 | |
| β-strand | 124 | 1 | 14 |
| α-helix | 125-126 | 2 | |
| β-strand | 127-132 | 6 | 11 |
| α-helix | 133-134 | 2 | |
| α-helix | 135-141 | 7 | |
| β-strand | 143-153 | 11 | 11 |
| β-strand | 154 | 1 | 14 |
| β-strand | 158-164 | 7 | 15 |
| β-strand | 167-169 | 3 | 15 |
| β-strand | 173-175 | 3 | 11 |
| β-strand | 180-181 | 2 | 11 |
| β-strand | 191-200 | 10 | 11 |
| α-helix | 201-204 | 4 | |
| β-strand | 210-217 | 8 | 15 |
| β-strand | 220 | 1 | 16 |
| α-helix | 231-232 | 2 | |
| β-strand | 234 | 1 | 16 |
| β-strand | 236-243 | 8 | 15 |
Chain F: 10 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-13 | 11 | 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 | 57-84 | 28 | |
| β-strand | 93-103 | 11 | 17 |
| β-strand | 109-118 | 10 | 17 |
| β-strand | 121-126 | 6 | 17 |
| β-strand | 133-135 | 3 | 17 |
| α-helix | 139-149 | 11 | |
| α-helix | 152-158 | 7 | |
| α-helix | 159-163 | 5 | |
| α-helix | 164-174 | 11 | |
| 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 | 222-223 | 2 | 20 |
| β-strand | 229-230 | 2 | 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 | 270-272 | 3 | 20 |
Chain G: 4 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 | 44-45 | 2 | 23 |
| α-helix | 46 | 1 | |
| 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 |
| α-helix | 90 | 1 | |
| β-strand | 91-94 | 4 | 23 |
Chain I: 5 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-4 | 2 | 24 |
| β-strand | 9-13 | 5 | 25 |
| β-strand | 17-24 | 8 | 24 |
| β-strand | 29-37 | 9 | 25 |
| α-helix | 42-43 | 2 | |
| β-strand | 44-49 | 6 | 25 |
| β-strand | 53-57 | 5 | 24 |
| β-strand | 62-67 | 6 | 24 |
| α-helix | 68-70 | 3 | |
| β-strand | 72-78 | 7 | 24 |
| α-helix | 82-84 | 3 | |
| β-strand | 86-94 | 9 | 25 |
| β-strand | 105-106 | 2 | 25 |
| β-strand | 110-115 | 6 | 25 |
| β-strand | 124-129 | 6 | 26 |
| β-strand | 130 | 1 | 27 |
| β-strand | 137-142 | 6 | 26 |
| α-helix | 151-153 | 3 | |
| β-strand | 159-160 | 2 | 26 |
| α-helix | 161-163 | 3 | |
| β-strand | 164-168 | 5 | 26 |
| β-strand | 173-181 | 9 | 26 |
9 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 |
|---|
| HLA-B35 | A, F, K, Q | protein | 276 | Homo sapiens | P01889 (AlphaFold model) |
| Beta-2-microglobulin | B, G, L, R | protein | 99 | Homo sapiens | P61769 (AlphaFold model) |
| EBV peptide, EPLPQGQLTAY | C, H, M, S | protein | 11 | | P03206 (AlphaFold model) |
| ELS4 TCR alpha chain | D, I, N, T | protein | 188 | Homo sapiens | P01848 (AlphaFold model) |
| ELS4 TCR beta chain | E, J, P, U | protein | 243 | Homo sapiens | P01850 |
Sequence of entity 1 (A, F, K, Q), FASTA
>2NX5_1 HLA-B35 (chains A, F, K, Q)
GSHSMRYFYTAMSRPGRGEPRFIAVGYVDDTQFVRFDSDAASPRTEPRAPWIEQEGPEYW
DRNTQIFKTNTQTYRESLRNLRGYYNQSEAGSHIIQRMYGCDLGPDGRLLRGHDQSAYDG
KDYIALNEDLSSWTAADTAAQITQRKWEAARVAEQLRAYLEGLCVEWLRRYLENGKETLQ
RADPPKTHVTHHPVSDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDRT
FQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEP
Sequence of entity 2 (B, G, L, R), FASTA
>2NX5_2 Beta-2-microglobulin (chains B, G, L, R)
IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDW
SFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
Sequence of entity 3 (C, H, M, S), FASTA
>2NX5_3 EBV peptide, EPLPQGQLTAY (chains C, H, M, S)
EPLPQGQLTAY
Sequence of entity 4 (D, I, N, T), FASTA
>2NX5_4 ELS4 TCR alpha chain (chains D, I, N, T)
QNIDQPTEMTATEGAIVQINCTYQTSGFNGLFWYQQHAGEAPTFLSYNVLDGLEEKGRFS
SFLSRSKGYSYLLLKELQMKDSASYLCAVQASGGSYIPTFGRGTSLIVHPYIQNPDPAVY
QLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLDMRSMDFKSNSAVAWSNKSD
FACANAFN
Sequence of entity 5 (E, J, P, U), FASTA
>2NX5_5 ELS4 TCR beta chain (chains E, J, P, U)
DAGITQSPRHKVTETGTPVTLRCHQTENHRYMYWYRQDPGHGLRLIHYSYGVKDTDKGEV
SDGYSVSRSKTEDFLLTLESATSSQTSVYFCATGTGDSNQPQHFGDGTRLSILEDLNKVF
PPEVAVFEPSEAEISHTQKATLVCLATGFFPDHVELSWWVNGKEVHSGVCTDPQPLKEQP
ALNDSRYALSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWG
RAD
Primary citation
A T cell receptor flattens a bulged antigenic peptide presented by a major histocompatibility complex class I molecule. Tynan, F.E., Reid, H.H., Kjer-Nielsen, L. et al. Nat Immunol (2007) 8:268-276. DOI 10.1038/ni1432 · PubMed
Other PDB entries of the same protein (UniProt P01889 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 1K5N 1.09 Å, HLA-B*2709 bound to nona-peptide M9
- 4U1M 1.18 Å, HLA class I micropolymorphisms determine peptide-HLA landscape and dictate differential…
- 3CZF 1.2 Å, Crystal structure of HLA-B*2709 complexed with the glucagon receptor (GR) peptide…
- 6MT3 1.21 Å, Crystal Structure of HLA-B*18:01 in complex with NP338 influenza peptide
- 3LN4 1.3 Å, Crystal structure of HLA-B*4103 in complex with a 16mer self-peptide derived from…
- 3BWA 1.3 Å, Crystal Structure of HLA B*3508 in complex with a HCMV 8-mer peptide from the pp65 protein
- 3SPV 1.3 Å, Crystal structure of a peptide-HLA complex
- 6MT6 1.31 Å, Crystal Structure of HLA-B*37:01 in complex with NP338 influenza peptide
- 2BVP 1.35 Å, Structures of Three HIV-1 HLA-B5703-Peptide Complexes and Identification of Related HLAs…
- 6MTL 1.35 Å, Crystal Structure of HLA-B*44:05 in complex with NP338 influenza peptide
- 4U1J 1.38 Å, HLA class I micropolymorphisms determine peptide-HLA landscape and dictate differential…
- 6PYW 1.38 Å, Crystal Structure of HLA-B*2705-W60A in complex with LRN, a self-peptide
Browse structure collections
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