2AK4: SB27 TCR
Crystal Structure of SB27 TCR in complex with HLA-B*3508-13mer peptide. Determined by X-ray diffraction at 2.5 Å resolution. Released 11 Oct 2005.
- Method
- X-ray diffraction
- Resolution
- 2.5 Å
- Organism
- Homo sapiens
- Chains
- 20
- Atoms
- 26,609
- Mol. weight
- 390.03 kDa
- Released
- 11 Oct 2005
Explore 2AK4 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
2AK4 contains 119 α-helices and 310 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: 12 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-12 | 9 | 1 |
| α-helix | 19-20 | 2 | |
| 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 |
| α-helix | 104 | 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 | 186-193 | 8 | 3 |
| β-strand | 198-208 | 11 | 3 |
| β-strand | 209 | 1 | 2 |
| β-strand | 214-219 | 6 | 4 |
| β-strand | 222-223 | 2 | 4 |
| α-helix | 225-227 | 3 | |
| β-strand | 229-230 | 2 | 3 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 3 |
| β-strand | 241-250 | 10 | 3 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-262 | 6 | 4 |
| β-strand | 270-272 | 3 | 4 |
Chains B, G, L and R: 4 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 |
| α-helix | 90 | 1 | |
| β-strand | 91-94 | 4 | 7 |
Chains C and H: 2 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 4-5 | 2 | |
| β-strand | 6 | 1 | 8 |
| α-helix | 9-12 | 4 | |
Chain D: 4 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-4 | 3 | 9 |
| β-strand | 9-13 | 5 | 10 |
| β-strand | 18-20 | 3 | 9 |
| β-strand | 23-25 | 3 | 9 |
| β-strand | 31-37 | 7 | 10 |
| β-strand | 44-50 | 7 | 10 |
| β-strand | 55-57A | 4 | 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 | 105-106 | 2 | 10 |
| β-strand | 110-115 | 6 | 10 |
| β-strand | 124-128 | 5 | 11 |
| β-strand | 129 | 1 | 12 |
| β-strand | 137-142 | 6 | 11 |
| α-helix | 150-153 | 4 | |
| β-strand | 159-160 | 2 | 11 |
| α-helix | 161-163 | 3 | |
| β-strand | 164-168 | 5 | 11 |
| α-helix | 169-171 | 3 | |
| β-strand | 173-182 | 10 | 11 |
| β-strand | 203 | 1 | 11 |
Chains E and J: 8 helices, 27 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-7 | 4 | 13 |
| β-strand | 10-14 | 5 | 14 |
| β-strand | 19-21 | 3 | 15 |
| β-strand | 22-25 | 4 | 13 |
| β-strand | 32-38 | 7 | 14 |
| β-strand | 42-51 | 10 | 14 |
| β-strand | 54-57 | 4 | 14 |
| β-strand | 66-68 | 3 | 15 |
| β-strand | 74 | 1 | 13 |
| β-strand | 76-79 | 4 | 15 |
| α-helix | 84-86 | 3 | |
| β-strand | 88-93 | 6 | 14 |
| β-strand | 108 | 1 | 14 |
| β-strand | 112-117 | 6 | 14 |
| α-helix | 120-122 | 3 | |
| β-strand | 124 | 1 | 16 |
| α-helix | 125-126 | 2 | |
| β-strand | 127-131 | 5 | 17 |
| β-strand | 132 | 1 | 12 |
| α-helix | 133-134 | 2 | |
| α-helix | 135-141 | 7 | |
| β-strand | 143-153 | 11 | 17 |
| β-strand | 154 | 1 | 16 |
| β-strand | 158-164 | 7 | 18 |
| β-strand | 167-169 | 3 | 18 |
| β-strand | 173-175 | 3 | 17 |
| α-helix | 179 | 1 | |
| β-strand | 180-181 | 2 | 17 |
| β-strand | 191-200 | 10 | 17 |
| α-helix | 201-204 | 4 | |
| β-strand | 210-217 | 8 | 18 |
| β-strand | 220 | 1 | 19 |
| α-helix | 231-232 | 2 | |
| β-strand | 234 | 1 | 19 |
| β-strand | 236-243 | 8 | 18 |
Chain F: 11 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-12 | 9 | 20 |
| α-helix | 19-20 | 2 | |
| β-strand | 21-28 | 8 | 20 |
| β-strand | 31-37 | 7 | 20 |
| β-strand | 46-47 | 2 | 20 |
| α-helix | 50-52 | 3 | |
| α-helix | 57-84 | 28 | |
| β-strand | 94-103 | 10 | 20 |
| β-strand | 109-118 | 10 | 20 |
| β-strand | 121-126 | 6 | 20 |
| β-strand | 133-135 | 3 | 20 |
| α-helix | 138-149 | 12 | |
| α-helix | 152-161 | 10 | |
| α-helix | 163-174 | 12 | |
| α-helix | 176-179 | 4 | |
| β-strand | 183 | 1 | 21 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-193 | 8 | 22 |
| β-strand | 198-208 | 11 | 22 |
| β-strand | 209 | 1 | 21 |
| β-strand | 214-219 | 6 | 23 |
| β-strand | 222-223 | 2 | 23 |
| α-helix | 225-227 | 3 | |
| β-strand | 229-230 | 2 | 22 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 22 |
| β-strand | 241-250 | 10 | 22 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-262 | 6 | 23 |
| β-strand | 270-272 | 3 | 23 |
Chain I: 5 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-4 | 3 | 28 |
| β-strand | 9-13 | 5 | 29 |
| β-strand | 18-20 | 3 | 28 |
| β-strand | 23-25 | 3 | 28 |
| β-strand | 31-37 | 7 | 29 |
| β-strand | 44-50 | 7 | 29 |
| β-strand | 55-57A | 4 | 28 |
| β-strand | 62-67 | 6 | 28 |
| β-strand | 72-77 | 6 | 28 |
| α-helix | 82-84 | 3 | |
| β-strand | 86-93 | 8 | 29 |
| β-strand | 96 | 1 | 27 |
| β-strand | 105-106 | 2 | 29 |
| β-strand | 110-115 | 6 | 29 |
| β-strand | 124-128 | 5 | 30 |
| β-strand | 129 | 1 | 31 |
| α-helix | 130-131 | 2 | |
| β-strand | 138-142 | 5 | 30 |
| α-helix | 150-153 | 4 | |
| β-strand | 159-160 | 2 | 30 |
| α-helix | 161-163 | 3 | |
| β-strand | 164-168 | 5 | 30 |
| α-helix | 169-171 | 3 | |
| β-strand | 173-181 | 9 | 30 |
| β-strand | 203 | 1 | 30 |
Chain K: 11 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-12 | 10 | 39 |
| α-helix | 19-20 | 2 | |
| β-strand | 21-28 | 8 | 39 |
| β-strand | 31-37 | 7 | 39 |
| β-strand | 46-47 | 2 | 39 |
| α-helix | 50-52 | 3 | |
| α-helix | 57-84 | 28 | |
| β-strand | 94-103 | 10 | 39 |
| β-strand | 109-118 | 10 | 39 |
| β-strand | 121-126 | 6 | 39 |
| β-strand | 133-135 | 3 | 39 |
| α-helix | 138-149 | 12 | |
| α-helix | 152-161 | 10 | |
| α-helix | 163-174 | 12 | |
| α-helix | 176-179 | 4 | |
| β-strand | 183 | 1 | 40 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-195 | 10 | 41 |
| β-strand | 198-208 | 11 | 41 |
| β-strand | 209 | 1 | 40 |
| β-strand | 214-219 | 6 | 42 |
| β-strand | 222-223 | 2 | 42 |
| α-helix | 225-227 | 3 | |
| β-strand | 229-230 | 2 | 41 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 41 |
| β-strand | 241-250 | 10 | 41 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-262 | 6 | 42 |
| β-strand | 270-272 | 3 | 42 |
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 |
|---|
| HLA-B35 variant | 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 LPEPLPQGQLTAY | C, H, M, S | protein | 13 | | P03206 (AlphaFold model) |
| SB27 T cell receptor alpha chain | D, I, N, T | protein | 211 | Homo sapiens | P01848 (AlphaFold model) |
| SB27 T cell receptor beta chain | E, J, P, U | protein | 245 | Homo sapiens | P01850 |
Sequence of entity 1 (A, F, K, Q), FASTA
>2AK4_1 HLA-B35 variant (chains A, F, K, Q)
GSHSMRYFYTAMSRPGRGEPRFIAVGYVDDTQFVRFDSDAASPRTEPRAPWIEQEGPEYW
DRNTQIFKTNTQTYRESLRNLRGYYNQSEAGSHIIQRMYGCDLGPDGRLLRGHDQSAYDG
KDYIALNEDLSSWTAADTAAQITQRKWEAARVAEQRRAYLEGLCVEWLRRYLENGKETLQ
RADPPKTHVTHHPVSDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDRT
FQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEP
Sequence of entity 2 (B, G, L, R), FASTA
>2AK4_2 Beta-2-microglobulin (chains B, G, L, R)
IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDW
SFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
Sequence of entity 3 (C, H, M, S), FASTA
>2AK4_3 EBV peptide LPEPLPQGQLTAY (chains C, H, M, S)
LPEPLPQGQLTAY
Sequence of entity 4 (D, I, N, T), FASTA
>2AK4_4 SB27 T cell receptor alpha chain (chains D, I, N, T)
HMAQKVTQAQTEISVVEKEDVTLDCVYETRDTTYYLFWYKQPPSGELVFLIRRNSFDEQN
EISGRYSWNFQKSTSSFNFTITASQVVDSAVYFCALSGFYNTDKLIFGTGTRLQVFPNIQ
NPDPAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLDMRSMDFKSNSAV
AWSNKSDFACANAFNNSIIPEDTFFPSPESS
Sequence of entity 5 (E, J, P, U), FASTA
>2AK4_5 SB27 T cell receptor beta chain (chains E, J, P, U)
HMNAGVTQTPKFQVLKTGQSMTLQCAQDMNHNSMYWYRQDPGMGLRLIYYSASEGTTDKG
EVPNGYNVSRLNKREFSLRLESAAPSQTSVYFCASPGLAGEYEQYFGPGTRLTVTEDLKN
VFPPEVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVCTDPQPLKE
QPALNDSRYALSSRLRVSATFWQNPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEA
WGRAD
Primary citation
T cell receptor recognition of a 'super-bulged' major histocompatibility complex class I-bound peptide. Tynan, F.E., Burrows, S.R., Buckle, A.M. et al. Nat Immunol (2005) 6:1114-1122. DOI 10.1038/ni1257 · 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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