6LF9: MHC class I antigen
Crystal structure of pSLA-1*1301 complex with dodecapeptide RVEDVTNTAEYW. Determined by X-ray diffraction at 2.5 Å resolution. Released 17 Mar 2021.
- Method
- X-ray diffraction
- Resolution
- 2.5 Å
- Organisms
- Sus scrofa, synthetic construct
- Chains
- 12
- Atoms
- 12,718
- Mol. weight
- 176.49 kDa
- Released
- 17 Mar 2021
Explore 6LF9 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6LF9 contains 54 α-helices and 117 β-strands across 8 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, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-13 | 10 | 8 |
| β-strand | 20-28 | 9 | 8 |
| β-strand | 31-37 | 7 | 8 |
| β-strand | 46-47 | 2 | 8 |
| α-helix | 51-54 | 4 | |
| α-helix | 57-85 | 29 | |
| β-strand | 94-103 | 10 | 8 |
| β-strand | 109-118 | 10 | 8 |
| β-strand | 121-126 | 6 | 8 |
| β-strand | 133-135 | 3 | 8 |
| α-helix | 140-150 | 11 | |
| α-helix | 152-158 | 7 | |
| α-helix | 159-164 | 6 | |
| α-helix | 165-174 | 10 | |
| α-helix | 176-179 | 4 | |
| α-helix | 181-182 | 2 | |
| β-strand | 183 | 1 | 9 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-193 | 8 | 10 |
| β-strand | 199-208 | 10 | 10 |
| β-strand | 209 | 1 | 9 |
| β-strand | 214-219 | 6 | 11 |
| α-helix | 225-227 | 3 | |
| β-strand | 229-230 | 2 | 10 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 10 |
| β-strand | 241-249 | 9 | 10 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-262 | 6 | 11 |
| β-strand | 270-272 | 3 | 11 |
Chain B: 3 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5 | 1 | 12 |
| α-helix | 6-7 | 2 | |
| β-strand | 8-13 | 6 | 13 |
| β-strand | 23-32 | 10 | 13 |
| β-strand | 33 | 1 | 12 |
| β-strand | 37-43 | 7 | 14 |
| β-strand | 46-47 | 2 | 14 |
| α-helix | 48-49 | 2 | |
| β-strand | 51-52 | 2 | 13 |
| α-helix | 53-55 | 3 | |
| β-strand | 56-57 | 2 | 13 |
| β-strand | 63-71 | 9 | 13 |
| β-strand | 79-85 | 7 | 14 |
| β-strand | 92-95 | 4 | 14 |
Chain D: 11 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-13 | 10 | 1 |
| β-strand | 20-28 | 9 | 1 |
| β-strand | 31-37 | 7 | 1 |
| β-strand | 46-47 | 2 | 1 |
| α-helix | 51-54 | 4 | |
| 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 | 159-164 | 6 | |
| α-helix | 165-174 | 10 | |
| α-helix | 176-179 | 4 | |
| 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 | 225 | 1 | 4 |
| α-helix | 226-227 | 2 | |
| β-strand | 229-230 | 2 | 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 |
Chains E, H and K: 3 helices, 11 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5 | 1 | 5 |
| α-helix | 6-7 | 2 | |
| β-strand | 8-13 | 6 | 6 |
| β-strand | 23-32 | 10 | 6 |
| β-strand | 33 | 1 | 5 |
| β-strand | 38-43 | 6 | 7 |
| β-strand | 46-47 | 2 | 7 |
| α-helix | 48-49 | 2 | |
| β-strand | 51-52 | 2 | 6 |
| α-helix | 53-55 | 3 | |
| β-strand | 56-57 | 2 | 6 |
| β-strand | 63-71 | 9 | 6 |
| β-strand | 79-84 | 6 | 7 |
| β-strand | 92-95 | 4 | 7 |
Chain G: 9 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-13 | 10 | 15 |
| β-strand | 20-28 | 9 | 15 |
| β-strand | 31-37 | 7 | 15 |
| β-strand | 46-47 | 2 | 15 |
| α-helix | 51-54 | 4 | |
| α-helix | 57-84 | 28 | |
| β-strand | 94-103 | 10 | 15 |
| β-strand | 109-118 | 10 | 15 |
| β-strand | 121-126 | 6 | 15 |
| β-strand | 133-135 | 3 | 15 |
| α-helix | 140-150 | 11 | |
| α-helix | 152-159 | 8 | |
| α-helix | 160-164 | 5 | |
| α-helix | 165-174 | 10 | |
| β-strand | 183 | 1 | 16 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-193 | 8 | 17 |
| β-strand | 199-208 | 10 | 17 |
| β-strand | 209 | 1 | 16 |
| β-strand | 214-219 | 6 | 18 |
| β-strand | 229-230 | 2 | 17 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 17 |
| β-strand | 241-249 | 9 | 17 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-262 | 6 | 18 |
| β-strand | 270-272 | 3 | 18 |
Chain J: 10 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-13 | 10 | 22 |
| β-strand | 20-28 | 9 | 22 |
| β-strand | 31-37 | 7 | 22 |
| β-strand | 46-47 | 2 | 22 |
| α-helix | 51-54 | 4 | |
| α-helix | 57-85 | 29 | |
| β-strand | 94-103 | 10 | 22 |
| β-strand | 109-118 | 10 | 22 |
| β-strand | 121-126 | 6 | 22 |
| β-strand | 133-135 | 3 | 22 |
| α-helix | 140-149 | 10 | |
| α-helix | 152-159 | 8 | |
| α-helix | 160-164 | 5 | |
| α-helix | 165-174 | 10 | |
| α-helix | 181-182 | 2 | |
| β-strand | 183 | 1 | 23 |
| α-helix | 184-185 | 2 | |
| β-strand | 186-193 | 8 | 24 |
| β-strand | 199-208 | 10 | 24 |
| β-strand | 209 | 1 | 23 |
| β-strand | 214-218 | 5 | 25 |
| β-strand | 229-230 | 2 | 24 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 24 |
| β-strand | 241-249 | 9 | 24 |
| α-helix | 254-256 | 3 | |
| β-strand | 258-262 | 5 | 25 |
| β-strand | 270-272 | 3 | 25 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| MHC class I antigen | A, D, G, J | protein | 273 | Sus scrofa | B1PJU7 (AlphaFold model) |
| Beta-2-microglobulin | B, E, H, K | protein | 97 | Sus scrofa | Q07717 (AlphaFold model) |
| Arg-val-glu-asp-val-thr-asn-thr-ala-glu-tyr-trp | C, F, I, L | protein | 12 | synthetic construct | P16082 |
Sequence of entity 1 (A, D, G, J), FASTA
>6LF9_1 MHC class I antigen (chains A, D, G, J)
GPHSLSYFYTAVSRPDRGDSRFIAVGYVDDTQFVRFDNYAPNPRMEPRVPWIQQEGQDYW
DEETRKVKDNAQTYGVGLNTLRGYYNQSEAGSHTLQSMFGCYLGPDGLLLHGYRQDAYDG
ADYIALNEDLRSWTAADMAAQITKRKWEAANVAERRRSYLQGLCVESLRRYLEMGKDTLQ
RAEPPKTHVTRHPSSDLGVTLRCWALGFYPKEISLTWQREGQDQSQDMELVETRPSGDGT
FQKWAALVVPPGEEQSYTCHVQHEGLQEPLTLR
Sequence of entity 2 (B, E, H, K), FASTA
>6LF9_2 Beta-2-microglobulin (chains B, E, H, K)
ARPPKVQVYSRHPAENGKPNYLNCYVSGFHPPQIEIDLLKNGEKMNAEQSDLSFSKDWSF
YLLVHTEFTPNAVDQYSCRVKHVTLDKPKIVKWDRDH
Sequence of entity 3 (C, F, I, L), FASTA
>6LF9_3 ARG-VAL-GLU-ASP-VAL-THR-ASN-THR-ALA-GLU-TYR-TRP (chains C, F, I, L)
RVEDVTNTAEYW
Primary citation
Peptidomes and Structures Illustrate How SLA-I Micropolymorphism Influences the Preference of Binding Peptide Length. Wei, X.H., Wang, S., Zhang, N.Z. et al. Front Immunol (2022). DOI 10.3389/fimmu.2022.820881
Other PDB entries of the same protein (UniProt B1PJU7 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6KWO 1.8 Å, Crystal structure of pSLA-1*1301 complex with mutant epitope ESDTVGWSW
- 6KWN 2.4 Å, Crystal structure of pSLA-1*1301(F99Y) complex with S-OIV-derived epitope NSDTVGWSW
Browse structure collections
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