6EWA: HLA-A2
Crystal structure of HLA-A2 in complex with LILRB1. Determined by X-ray diffraction at 2.39 Å resolution. Released 7 Nov 2018.
- Method
- X-ray diffraction
- Resolution
- 2.39 Å
- Organisms
- Homo sapiens, Human immunodeficiency virus 1
- Chains
- 8
- Atoms
- 9,148
- Mol. weight
- 132.88 kDa
- Released
- 7 Nov 2018
Explore 6EWA in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6EWA contains 35 α-helices and 107 β-strands across 6 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: 10 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-12 | 10 | 1 |
| β-strand | 21-28 | 8 | 1 |
| β-strand | 31-37 | 7 | 1 |
| β-strand | 46-47 | 2 | 1 |
| α-helix | 50-53 | 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 | 133-134 | 2 | 1 |
| α-helix | 139-149 | 11 | |
| 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 | 198-208 | 11 | 3 |
| β-strand | 209 | 1 | 2 |
| β-strand | 214-219 | 6 | 4 |
| β-strand | 222-223 | 2 | 4 |
| 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 | 270-273 | 4 | 4 |
Chain B: 2 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2 | 1 | 5 |
| β-strand | 3 | 1 | 6 |
| α-helix | 4-5 | 2 | |
| β-strand | 6-11 | 6 | 7 |
| β-strand | 21-30 | 10 | 7 |
| β-strand | 31 | 1 | 6 |
| β-strand | 36-41 | 6 | 8 |
| β-strand | 44-45 | 2 | 8 |
| α-helix | 46 | 1 | |
| β-strand | 50-51 | 2 | 7 |
| β-strand | 55-56 | 2 | 7 |
| β-strand | 62-70 | 9 | 7 |
| β-strand | 78-83 | 6 | 8 |
| β-strand | 87 | 1 | 9 |
| β-strand | 91-94 | 4 | 8 |
Chain D: 4 helices, 21 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-11 | 4 | 10 |
| β-strand | 15-17 | 3 | 11 |
| β-strand | 22-26 | 5 | 10 |
| β-strand | 38-39 | 2 | 12 |
| α-helix | 47-49 | 3 | |
| β-strand | 61-62 | 2 | 10 |
| α-helix | 67-69 | 3 | |
| β-strand | 71-74 | 4 | 12 |
| α-helix | 86-90 | 5 | |
| β-strand | 91-93 | 3 | 12 |
| β-strand | 94-96 | 3 | 11 |
| β-strand | 99 | 1 | 9 |
| β-strand | 103-107 | 5 | 13 |
| β-strand | 111-113 | 3 | 14 |
| β-strand | 118-123 | 6 | 13 |
| β-strand | 126 | 1 | 5 |
| β-strand | 130-136 | 7 | 15 |
| β-strand | 143-147 | 5 | 15 |
| β-strand | 156-161 | 6 | 13 |
| β-strand | 171-177 | 7 | 15 |
| β-strand | 184 | 1 | 11 |
| β-strand | 185 | 1 | 15 |
| α-helix | 186-191 | 6 | |
| β-strand | 192-193 | 2 | 15 |
| β-strand | 195-197 | 3 | 14 |
Chain E: 11 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-12 | 10 | 16 |
| α-helix | 20 | 1 | |
| β-strand | 21-28 | 8 | 16 |
| β-strand | 31-37 | 7 | 16 |
| β-strand | 46-47 | 2 | 16 |
| α-helix | 50-53 | 4 | |
| α-helix | 57-84 | 28 | |
| β-strand | 94-103 | 10 | 16 |
| β-strand | 109-118 | 10 | 16 |
| β-strand | 121-126 | 6 | 16 |
| β-strand | 133-135 | 3 | 16 |
| α-helix | 141-149 | 9 | |
| α-helix | 152-158 | 7 | |
| α-helix | 159-163 | 5 | |
| α-helix | 164-174 | 11 | |
| α-helix | 176-179 | 4 | |
| β-strand | 183 | 1 | 17 |
| β-strand | 186-195 | 10 | 18 |
| β-strand | 198-208 | 11 | 18 |
| β-strand | 209 | 1 | 17 |
| β-strand | 214-219 | 6 | 19 |
| β-strand | 222-223 | 2 | 19 |
| α-helix | 225-227 | 3 | |
| β-strand | 228-230 | 3 | 18 |
| α-helix | 231-233 | 3 | |
| β-strand | 234-235 | 2 | 18 |
| β-strand | 241-249 | 9 | 18 |
| α-helix | 254-256 | 3 | |
| β-strand | 257-262 | 6 | 19 |
| β-strand | 270-272 | 3 | 19 |
Chain F: 3 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2 | 1 | 20 |
| 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 |
| β-strand | 87 | 1 | 24 |
| β-strand | 91-94 | 4 | 23 |
Chain H: 5 helices, 22 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-11 | 5 | 25 |
| β-strand | 15-17 | 3 | 26 |
| β-strand | 22-27 | 6 | 25 |
| β-strand | 35-39 | 5 | 27 |
| α-helix | 45-47 | 3 | |
| α-helix | 52-56 | 5 | |
| β-strand | 59-62 | 4 | 25 |
| α-helix | 67-69 | 3 | |
| β-strand | 71-77 | 7 | 27 |
| β-strand | 78-79 | 2 | 28 |
| β-strand | 83-84 | 2 | 28 |
| α-helix | 85-90 | 6 | |
| β-strand | 91-93 | 3 | 27 |
| β-strand | 94-96 | 3 | 26 |
| β-strand | 99 | 1 | 24 |
| β-strand | 103-107 | 5 | 29 |
| β-strand | 111-113 | 3 | 30 |
| β-strand | 119-123 | 5 | 29 |
| β-strand | 126 | 1 | 20 |
| β-strand | 130-136 | 7 | 26 |
| β-strand | 144-147 | 4 | 26 |
| β-strand | 156-160 | 5 | 29 |
| β-strand | 171-177 | 7 | 26 |
| β-strand | 184-185 | 2 | 26 |
| α-helix | 187-191 | 5 | |
| β-strand | 192-193 | 2 | 26 |
| β-strand | 195-197 | 3 | 30 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| HLA class I histocompatibility antigen, A-2 alpha chain | A, E | protein | 276 | Homo sapiens | P04439 (AlphaFold model) |
| Beta-2-microglobulin | B, F | protein | 99 | Homo sapiens | P61769 (AlphaFold model) |
| Polyprotein | C, G | protein | 9 | Human immunodeficiency virus 1 | P04585 (AlphaFold model) |
| LIR-1 | D, H | protein | 195 | Homo sapiens | Q8NHL6 (AlphaFold model) |
Sequence of entity 1 (A, E), FASTA
>6EWA_1 HLA class I histocompatibility antigen, A-2 alpha chain (chains A, E)
GSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYW
DGETRKVKAHSQTHRVDLGTLRGYYNQSEAGSHTVQRMYGCDVGSDWRFLRGYHQYAYDG
KDYIALKEDLRSWTAADMAAQTTKHKWEAAHVAEQLRAYLEGTCVEWLRRYLENGKETLQ
RTDAPKTHMTHHAVSDHEATLRCWALSFYPAEITLTWQRDGEDQTQDTELVETRPAGDGT
FQKWAAVVVPSGQEQRYTCHVQHEGLPKPLTLRWEP
Sequence of entity 2 (B, F), FASTA
>6EWA_2 Beta-2-microglobulin (chains B, F)
IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDW
SFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
Sequence of entity 3 (C, G), FASTA
>6EWA_3 Polyprotein (chains C, G)
ILKEPVHGV
Sequence of entity 4 (D, H), FASTA
>6EWA_4 LIR-1 (chains D, H)
PKPTLWAEPGSVITQGSPVTLRCQGGQETQEYRLYREKKTAPWITRIPQELVKKGQFPIP
SITWEHAGRYRCYYGSDTAGRSESSDPLELVVTGAYIKPTLSAQPSPVVNSGGNVTLQCD
SQVAFDGFILCKEGEDEHPQCLNSQPHARGSSRAIFSVGPVSPSRRWWYRCYAYDSNSPY
EWSLPSDLLELLVLG
Primary citation
Application of the immunoregulatory receptor LILRB1 as a crystallisation chaperone for human class I MHC complexes. Mohammed, F., Stones, D.H., Willcox, B.E. J Immunol Methods (2019) 464:47-56. DOI 10.1016/j.jim.2018.10.011 · PubMed
Other PDB entries of the same protein (UniProt P04439 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 3MRE 1.1 Å, Crystal Structure of MHC class I HLA-A2 molecule complexed with EBV bmlf1-280-288…
- 3D25 1.3 Å, Crystal structure of HA-1 minor histocompatibility antigen bound to human class I MHC…
- 3MRG 1.3 Å, Crystal Structure of MHC class I HLA-A2 molecule complexed with HCV NS3-1073-1081…
- 6JOZ 1.35 Å, Crystal structure of BRLF peptide from EBV in complex with HLA-A1101.
- 5C0G 1.37 Å, HLA-A02 carrying YLGGPDFPTI
- 5N1Y 1.39 Å, HLA-A02 carrying MVWGPDPLYV
- 1I4F 1.4 Å, Crystal structure of HLA-A*0201/MAGE-A4-peptide complex
- 1OGA 1.4 Å, A structural basis for immunodominant human T-cell receptor recognition.
- 3MRB 1.4 Å, Crystal Structure of MHC class I HLA-A2 molecule complexed with HCMV pp65-495-503…
- 3MRK 1.4 Å, Crystal Structure of MHC class I HLA-A2 molecule complexed with AFP137 nonapeptide
- 6J2A 1.4 Å, The structure of HLA-A*3003/NP44
- 1X7Q 1.45 Å, Crystal structure of HLA-A*1101 with sars nucleocapsid peptide
Browse structure collections
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