4MJI: PDB entry 4MJI
T cell response to a HIV reverse transcriptase epitope presented by the protective allele HLA-B*51:01. Determined by X-ray diffraction at 2.99 Å resolution. Released 28 May 2014.
- Method
- X-ray diffraction
- Resolution
- 2.99 Å
- Organisms
- Homo sapiens, Human immunodeficiency virus 1
- Chains
- 10
- Atoms
- 13,067
- Mol. weight
- 186.35 kDa
- Released
- 28 May 2014
Explore 4MJI in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4MJI contains 42 α-helices and 147 β-strands across 9 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: 8 helices, 18 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 | 50-52 | 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 | 152-159 | 8 | |
| α-helix | 160-164 | 5 | |
| α-helix | 165-174 | 10 | |
| α-helix | 176-179 | 4 | |
| β-strand | 183 | 1 | 2 |
| β-strand | 188-193 | 6 | 3 |
| β-strand | 198-208 | 11 | 3 |
| β-strand | 209 | 1 | 2 |
| β-strand | 214-219 | 6 | 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 | 270-272 | 3 | 4 |
Chain B: 2 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3 | 1 | 5 |
| α-helix | 4-5 | 2 | |
| β-strand | 6 | 1 | 6 |
| β-strand | 9-11 | 3 | 6 |
| β-strand | 21-30 | 10 | 6 |
| β-strand | 31 | 1 | 5 |
| β-strand | 36-41 | 6 | 7 |
| β-strand | 45 | 1 | 7 |
| β-strand | 50 | 1 | 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 |
Chain C: 1 helix, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 5-7 | 3 | |
Chain D: 5 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 11-14 | 4 | 8 |
| α-helix | 18-19 | 2 | |
| β-strand | 20-24 | 5 | 9 |
| β-strand | 32-38 | 7 | 8 |
| β-strand | 48-50 | 3 | 8 |
| β-strand | 55-58 | 4 | 9 |
| β-strand | 61-66 | 6 | 9 |
| β-strand | 71-76 | 6 | 9 |
| α-helix | 81-83 | 3 | |
| β-strand | 85-92 | 8 | 8 |
| β-strand | 99-101 | 3 | 8 |
| β-strand | 105-110 | 6 | 8 |
| β-strand | 119-125 | 7 | 10 |
| β-strand | 132-137 | 6 | 10 |
| β-strand | 150 | 1 | 11 |
| β-strand | 153 | 1 | 11 |
| β-strand | 154-155 | 2 | 10 |
| α-helix | 156-158 | 3 | |
| β-strand | 160-163 | 4 | 12 |
| α-helix | 164-166 | 3 | |
| β-strand | 168-171 | 4 | 12 |
| β-strand | 172-177 | 6 | 10 |
| α-helix | 184-187 | 4 | |
Chain E: 5 helices, 24 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 8-10 | 3 | 13 |
| β-strand | 13-17 | 5 | 14 |
| β-strand | 22-27 | 6 | 13 |
| β-strand | 34-40 | 7 | 14 |
| β-strand | 47-53 | 7 | 14 |
| β-strand | 56-59 | 4 | 14 |
| β-strand | 68-71 | 4 | 13 |
| β-strand | 78-82 | 5 | 13 |
| α-helix | 87-89 | 3 | |
| β-strand | 91-97 | 7 | 14 |
| β-strand | 106-107 | 2 | 14 |
| β-strand | 111-116 | 6 | 14 |
| β-strand | 123 | 1 | 15 |
| α-helix | 124-125 | 2 | |
| β-strand | 126-131 | 6 | 10 |
| α-helix | 132-133 | 2 | |
| α-helix | 134-139 | 6 | |
| β-strand | 142-152 | 11 | 10 |
| β-strand | 153 | 1 | 15 |
| β-strand | 157-163 | 7 | 16 |
| β-strand | 166-167 | 2 | 16 |
| β-strand | 172-174 | 3 | 10 |
| β-strand | 179-180 | 2 | 10 |
| β-strand | 190-199 | 10 | 10 |
| α-helix | 200-204 | 5 | |
| β-strand | 209-216 | 8 | 16 |
| β-strand | 219 | 1 | 17 |
| β-strand | 233 | 1 | 17 |
| β-strand | 236-242 | 7 | 16 |
Chain F: 7 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-14 | 12 | 18 |
| β-strand | 18-28 | 11 | 18 |
| β-strand | 31-37 | 7 | 18 |
| β-strand | 46-47 | 2 | 18 |
| α-helix | 50-52 | 3 | |
| α-helix | 57-84 | 28 | |
| β-strand | 94-103 | 10 | 18 |
| β-strand | 109-118 | 10 | 18 |
| β-strand | 121-126 | 6 | 18 |
| β-strand | 133-135 | 3 | 18 |
| α-helix | 138-149 | 12 | |
| α-helix | 152-159 | 8 | |
| α-helix | 160-164 | 5 | |
| α-helix | 165-174 | 10 | |
| α-helix | 176-179 | 4 | |
| β-strand | 183 | 1 | 19 |
| β-strand | 186-193 | 8 | 20 |
| β-strand | 198-208 | 11 | 20 |
| β-strand | 209 | 1 | 19 |
| β-strand | 214-219 | 6 | 21 |
| β-strand | 228-230 | 3 | 20 |
| β-strand | 234-235 | 2 | 20 |
| β-strand | 241-250 | 10 | 20 |
| β-strand | 257-262 | 6 | 21 |
| β-strand | 270-272 | 3 | 21 |
Chain G: 2 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3 | 1 | 22 |
| β-strand | 6 | 1 | 23 |
| β-strand | 9-11 | 3 | 23 |
| β-strand | 21-30 | 10 | 23 |
| β-strand | 31 | 1 | 22 |
| β-strand | 36-41 | 6 | 24 |
| β-strand | 45 | 1 | 24 |
| β-strand | 50 | 1 | 23 |
| α-helix | 52-54 | 3 | |
| β-strand | 55-56 | 2 | 23 |
| β-strand | 62-70 | 9 | 23 |
| β-strand | 78-83 | 6 | 24 |
| β-strand | 91-94 | 4 | 24 |
| α-helix | 95-96 | 2 | |
Chain I: 6 helices, 19 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 11-14 | 4 | 25 |
| α-helix | 18 | 1 | |
| β-strand | 19-24 | 6 | 26 |
| β-strand | 30-38 | 9 | 27 |
| β-strand | 45 | 1 | 27 |
| β-strand | 48-50 | 3 | 27 |
| β-strand | 55-58 | 4 | 26 |
| β-strand | 61-66 | 6 | 26 |
| β-strand | 71-76 | 6 | 26 |
| α-helix | 81-83 | 3 | |
| β-strand | 86-93 | 8 | 27 |
| β-strand | 99-101 | 3 | 27 |
| β-strand | 106 | 1 | 27 |
| β-strand | 107-110 | 4 | 25 |
| β-strand | 119-121 | 3 | 28 |
| β-strand | 125 | 1 | 29 |
| β-strand | 133-137 | 5 | 28 |
| α-helix | 143-145 | 3 | |
| β-strand | 154-155 | 2 | 28 |
| α-helix | 156-158 | 3 | |
| β-strand | 160-163 | 4 | 30 |
| α-helix | 164-166 | 3 | |
| β-strand | 168-171 | 4 | 30 |
| β-strand | 172-176 | 5 | 28 |
| α-helix | 184-187 | 4 | |
1 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 class I histocompatibility antigen, B-51 alpha chain | A, F | protein | 276 | Homo sapiens | P01889 (AlphaFold model) |
| Beta-2-microglobulin | B, G | protein | 99 | Homo sapiens | P61769 (AlphaFold model) |
| HIV Reverse Transcriptase peptide Marker | C, H | protein | 8 | Human immunodeficiency virus 1 | R4WL38 |
| T-Cell Receptor Chain alpha | D, I | protein | 195 | Homo sapiens | K7N5M3 (AlphaFold model) |
| T-cell Receptor Beta chain | E, J | protein | 242 | Homo sapiens | P01850 |
Sequence of entity 1 (A, F), FASTA
>4MJI_1 HLA class I histocompatibility antigen, B-51 alpha chain (chains A, F)
GSHSMRYFYTAMSRPGRGEPRFIAVGYVDDTQFVRFDSDAASPRTEPRAPWIEQEGPEYW
DRNTQIFKTNTQTYRENLRIALRYYNQSEAGSHTWQTMYGCDVGPDGRLLRGHNQYAYDG
KDYIALNEDLSSWTAADTAAQITQRKWEAAREAEQLRAYLEGLCVEWLRRHLENGKETLQ
RADPPKTHVTHHPVSDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDRT
FQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEP
Sequence of entity 2 (B, G), FASTA
>4MJI_2 Beta-2-microglobulin (chains B, G)
IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDW
SFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
Sequence of entity 3 (C, H), FASTA
>4MJI_3 HIV Reverse Transcriptase peptide Marker (chains C, H)
TAFTIPSI
Sequence of entity 4 (D, I), FASTA
>4MJI_4 T-Cell Receptor Chain alpha (chains D, I)
GEEDPQALSIQEGENATMNCSYKTSINNLQWYRQNSGRGLVHLILIRSNEREKHSGRLRV
TLDTSKKSSSLLITASRAADTASYFCATDDDSARQLTFGSGTQLTVLPDIQNPDPAVYQL
RDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKCVLDMRSMDFKSNSAVAWSNKSDFA
CANAFNNSIIPEDTF
Sequence of entity 5 (E, J), FASTA
>4MJI_5 T-cell Receptor Beta chain (chains E, J)
AGVSQTPSNKVTEKGKYVELRCDPISGHTALYWYRQSLGQGPEFLIYFQGTGAADDSGLP
NDRFFAVRPEGSVSTLKIQRTERGDSAVYLCASSLTGGGELFFGEGSRLTVLEDLKNVFP
PEVAVFEPSEAEISHTQKATLVCLATGFYPDHVELSWWVNGKEVHSGVCTDPQPLKEQPA
LNDSRYALSSRLRVSATFWQDPRNHFRCQVQFYGLSENDEWTQDRAKPVTQIVSAEAWGR
AD
Primary citation
Molecular basis of a dominant T cell response to an HIV reverse transcriptase 8-mer epitope presented by the protective allele HLA-B*51:01. Motozono, C., Kuse, N., Sun, X. et al. J Immunol (2014) 192:3428-3434. DOI 10.4049/jimmunol.1302667 · 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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