CryoEM structure of anti-MHC-I Fab M1/42 complex with H2-Dd. Determined by electron microscopy at 2.67 Å resolution. Released 4 Feb 2026.
Explore 9D72 in 3D Show helices and sheets RCSB PDB PDBe
9D72 contains 13 α-helices and 74 β-strands across 4 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-12 | 10 | 11 |
| α-helix | 20 | 1 | |
| β-strand | 21-28 | 8 | 11 |
| β-strand | 31-35 | 5 | 11 |
| β-strand | 37 | 1 | 11 |
| β-strand | 46-47 | 2 | 11 |
| α-helix | 50-52 | 3 | |
| α-helix | 57-84 | 28 | |
| β-strand | 96-103 | 8 | 11 |
| β-strand | 109-118 | 10 | 11 |
| β-strand | 121-126 | 6 | 11 |
| β-strand | 133-135 | 3 | 11 |
| 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 | |
| β-strand | 183 | 1 | 12 |
| β-strand | 186-189 | 4 | 13 |
| β-strand | 202-208 | 7 | 13 |
| β-strand | 209 | 1 | 12 |
| β-strand | 214-218 | 5 | 14 |
| β-strand | 228-230 | 3 | 13 |
| β-strand | 234-235 | 2 | 13 |
| β-strand | 241-247 | 7 | 13 |
| β-strand | 258-262 | 5 | 14 |
| β-strand | 270-272 | 3 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3 | 1 | 1 |
| β-strand | 6-8 | 3 | 2 |
| β-strand | 11 | 1 | 2 |
| β-strand | 16 | 1 | 3 |
| β-strand | 19 | 1 | 3 |
| β-strand | 21-30 | 10 | 2 |
| β-strand | 31 | 1 | 1 |
| β-strand | 36-39 | 4 | 4 |
| β-strand | 40-41 | 2 | 5 |
| β-strand | 44-45 | 2 | 5 |
| β-strand | 51-56 | 6 | 2 |
| β-strand | 62-70 | 9 | 2 |
| β-strand | 80-83 | 4 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5-7 | 3 | 15 |
| β-strand | 12 | 1 | 16 |
| β-strand | 16-23 | 8 | 15 |
| β-strand | 35-42 | 8 | 17 |
| β-strand | 48-54 | 7 | 17 |
| β-strand | 59-61 | 3 | 17 |
| β-strand | 69-73 | 5 | 15 |
| β-strand | 79-87 | 9 | 15 |
| β-strand | 93-100 | 8 | 17 |
| β-strand | 101-103 | 3 | 18 |
| β-strand | 106-108 | 3 | 18 |
| β-strand | 113 | 1 | 17 |
| β-strand | 117-119 | 3 | 17 |
| β-strand | 121 | 1 | 16 |
| β-strand | 130-134 | 5 | 19 |
| β-strand | 147-155 | 9 | 19 |
| β-strand | 161-164 | 4 | 20 |
| β-strand | 173-175 | 3 | 19 |
| β-strand | 179-181 | 3 | 19 |
| β-strand | 184-192 | 9 | 19 |
| β-strand | 204-209 | 6 | 20 |
| α-helix | 210-212 | 3 | |
| β-strand | 214-219 | 6 | 20 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6-7 | 2 | 6 |
| β-strand | 10-12 | 3 | 7 |
| β-strand | 19-23 | 5 | 6 |
| β-strand | 34-38 | 5 | 7 |
| β-strand | 45-49 | 5 | 7 |
| β-strand | 53-54 | 2 | 7 |
| α-helix | 55 | 1 | |
| β-strand | 64-67 | 4 | 6 |
| β-strand | 70-75 | 6 | 6 |
| β-strand | 85-89 | 5 | 7 |
| β-strand | 98 | 1 | 7 |
| β-strand | 102-105 | 4 | 7 |
| β-strand | 116-118 | 3 | 8 |
| α-helix | 119-121 | 3 | |
| α-helix | 122-127 | 6 | |
| β-strand | 129-139 | 11 | 8 |
| β-strand | 145-146 | 2 | 9 |
| β-strand | 150 | 1 | 10 |
| β-strand | 153 | 1 | 10 |
| β-strand | 160-163 | 4 | 8 |
| β-strand | 173-182 | 10 | 8 |
| α-helix | 183-188 | 6 | |
| β-strand | 191-197 | 7 | 9 |
| β-strand | 204-210 | 7 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Beta-2-microglobulin | B | protein | 98 | Mus musculus | P01887 (AlphaFold model) |
| Fab M1/42 Light Chain | L | protein | 213 | Rattus norvegicus | |
| Surface protein gp120 | P | protein | 10 | synthetic construct | P04582 |
| H-2 class I histocompatibility antigen, D-D alpha chain | A | protein | 273 | Mus musculus | P01900 (AlphaFold model) |
| Fab M1/42 Heavy Chain | H | protein | 222 | Rattus norvegicus |
>9D72_1 Beta-2-microglobulin (chains B) IQKTPQIQVYSRHPPENGKPNILNCYVTQFHPPHIEIQMLKNGKKIPKVEMSDMSFSKDW SFYILAHTEFTPTETDTYACRVKHASMAEPKTVYWDRD
>9D72_2 Fab M1/42 Light Chain (chains L) DIQMTQSPSSMSASLGDKVTINCLASEDIGNYLSWYQQRPGKSPKLMIYGVTNLEDGVPS RFSGSRSGSDYSLTINSLGYDDEGIYHCHEYYEYPFTFGSGTKLEIKRADAAPTVSIFPP STEQLATGGASVVCLMNNFYPRDISVKWKIDGTERRDGVLDSVTDQDSKDSTYSMSSTLS LTKADYESHNLYTCEVVHKTSSSPVVKSFNRNE
>9D72_3 Surface protein gp120 (chains P) RGPGRAFVTI
>9D72_4 H-2 class I histocompatibility antigen, D-D alpha chain (chains A) SHSLRYFVTAVSRPGFGEPRYMEVGYVDNTEFVRFDSDAENPRYEPRARWIEQEGPEYWE RETRRAKGNEQSFRVDLRTALRYYNQSAGGSHTLQWMAGCDVESDGRLLRGYWQFAYDGC DYIALNEDLKTWTAADMAAQITRRKWEQAGAAERDRAYLEGECVEWLRRYLKNGNATLLR TDPPKAHVTHHRRPEGDVTLRCWALGFYPADITLTWQLNGEELTQEMELVETRPAGDGTF QKWASVVVPLGKEQKYTCHVEHEGLPEPLTLRW
>9D72_5 Fab M1/42 Heavy Chain (chains H) QVTLKESGPGMLQPSKTLSLTCSFSGFSLSTSGLVVNWIRQPSGKSLEWLAAIDWDGDEY YNPSPKSRLTVSKDTSNTQVFLKITSVDTVDTATYYCARSRRYGRYSGAFDYWGLGVMVT VSSAETTAPSVYPLAPGTALKSNSMVTLGCLVKGYFPEPVTVTWNSGALSSGVHTFPAVL QSGLYTLTSSVTVPSSTWSSQAVTCNVAHPASSTKVDKKIVP
Structural mechanism of anti-MHC-I antibody blocking of inhibitory NK cell receptors in tumor immunity. Jiang, J., Panda, A.K., Natarajan, K. et al. Res Sq (2025). DOI 10.21203/rs.3.rs-7133881/v1 · PubMed
Other PDB entries of the same protein (UniProt P01887 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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