crystal structure of a human leukocyte antigen-A (HLA-G) blocking antibody. Determined by X-ray diffraction at 3.45 Å resolution. Released 22 Jul 2026.
Explore 9RWI in 3D Show helices and sheets RCSB PDB PDBe
9RWI contains 21 α-helices and 77 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 | 27-36 | 10 | 1 |
| β-strand | 45-52 | 8 | 1 |
| β-strand | 55-61 | 7 | 1 |
| β-strand | 70-71 | 2 | 1 |
| α-helix | 81-108 | 28 | |
| β-strand | 118-127 | 10 | 1 |
| β-strand | 133-142 | 10 | 1 |
| β-strand | 146-150 | 5 | 1 |
| β-strand | 157-159 | 3 | 1 |
| α-helix | 172-174 | 3 | |
| α-helix | 176-182 | 7 | |
| α-helix | 183-187 | 5 | |
| α-helix | 188-198 | 11 | |
| α-helix | 200-203 | 4 | |
| β-strand | 207 | 1 | 2 |
| α-helix | 208-209 | 2 | |
| β-strand | 213-217 | 5 | 3 |
| β-strand | 222-227 | 6 | 3 |
| β-strand | 232 | 1 | 4 |
| β-strand | 233 | 1 | 2 |
| β-strand | 237-243 | 7 | 5 |
| β-strand | 247 | 1 | 5 |
| β-strand | 252-254 | 3 | 3 |
| α-helix | 255-257 | 3 | |
| β-strand | 258-259 | 2 | 4 |
| β-strand | 265-266 | 2 | 4 |
| β-strand | 269-274 | 6 | 3 |
| α-helix | 278-280 | 3 | |
| β-strand | 281-287 | 7 | 5 |
| β-strand | 294-296 | 3 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 23-25 | 3 | |
| β-strand | 26-31 | 6 | 6 |
| β-strand | 42-50 | 9 | 6 |
| β-strand | 56-61 | 6 | 7 |
| β-strand | 70 | 1 | 6 |
| β-strand | 75-76 | 2 | 6 |
| β-strand | 82-89 | 8 | 6 |
| β-strand | 98-103 | 6 | 7 |
| β-strand | 112-113 | 2 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 8 |
| β-strand | 9-11 | 3 | 9 |
| β-strand | 17 | 1 | 10 |
| β-strand | 20-24 | 5 | 8 |
| β-strand | 33-38 | 6 | 9 |
| β-strand | 44-50 | 7 | 9 |
| β-strand | 56-58 | 3 | 9 |
| β-strand | 63 | 1 | 11 |
| β-strand | 66 | 1 | 11 |
| β-strand | 69-71 | 3 | 8 |
| α-helix | 72-74 | 3 | |
| β-strand | 76-78 | 3 | 8 |
| β-strand | 81 | 1 | 10 |
| β-strand | 88-94 | 7 | 9 |
| β-strand | 103 | 1 | 9 |
| β-strand | 108-112 | 5 | 9 |
| α-helix | 115-117 | 3 | |
| β-strand | 118 | 1 | 12 |
| α-helix | 119-120 | 2 | |
| β-strand | 121-125 | 5 | 13 |
| β-strand | 138-146 | 9 | 13 |
| β-strand | 147 | 1 | 12 |
| β-strand | 152-155 | 4 | 14 |
| β-strand | 160 | 1 | 14 |
| β-strand | 164-166 | 3 | 13 |
| α-helix | 167-169 | 3 | |
| β-strand | 170-171 | 2 | 13 |
| β-strand | 177-184 | 8 | 13 |
| β-strand | 192-198 | 7 | 14 |
| α-helix | 199-201 | 3 | |
| β-strand | 203-209 | 7 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 4-7 | 4 | 15 |
| β-strand | 10-14 | 5 | 16 |
| β-strand | 18 | 1 | 17 |
| β-strand | 21-25 | 5 | 15 |
| β-strand | 33-38 | 6 | 18 |
| α-helix | 43-44 | 2 | |
| β-strand | 45-49 | 5 | 18 |
| β-strand | 53-54 | 2 | 18 |
| β-strand | 63-66 | 4 | 15 |
| β-strand | 70-74 | 5 | 15 |
| β-strand | 76 | 1 | 17 |
| α-helix | 80-82 | 3 | |
| β-strand | 85-90 | 6 | 18 |
| β-strand | 101 | 1 | 18 |
| β-strand | 105 | 1 | 18 |
| β-strand | 106-110 | 5 | 16 |
| β-strand | 118-121 | 4 | 19 |
| α-helix | 122-124 | 3 | |
| α-helix | 127-130 | 4 | |
| β-strand | 132-142 | 11 | 19 |
| β-strand | 147-152 | 6 | 20 |
| β-strand | 155-156 | 2 | 20 |
| α-helix | 157 | 1 | |
| β-strand | 161-165 | 5 | 19 |
| α-helix | 166-169 | 4 | |
| β-strand | 175-184 | 10 | 19 |
| β-strand | 194-200 | 7 | 20 |
| β-strand | 203-209 | 7 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histone H2AX | P | protein | 8 | Homo sapiens | P16104 (AlphaFold model) |
| HLA class I histocompatibility antigen, alpha chain G | A | protein | 275 | Homo sapiens | P17693 (AlphaFold model) |
| Beta-2-microglobulin | B | protein | 99 | Homo sapiens | P61769 (AlphaFold model) |
| Fab heavy chain | H | protein | 212 | Oryctolagus cuniculus | |
| Fab light chain | L | protein | 213 | Oryctolagus cuniculus |
>9RWI_1 Histone H2AX (chains P) IIPRHLQL
>9RWI_2 HLA class I histocompatibility antigen, alpha chain G (chains A) SHSMRYFSAAVSRPGRGEPRFIAMGYVDDTQFVRFDSDSASPRMEPRAPWVEQEGPEYWE EETRNTKAHAQTDRMNLQTLRGYYNQSEASSHTLQWMIGCDLGSDGRLLRGYEQYAYDGK DYLALNEDLRSWTAADTAAQISKRKCEAANVAEQRRAYLEGTCVEWLHRYLENGKEMLQR ADPPKTHVTHHPVFDYEATLRCWALGFYPAEIILTWQRDGEDQTQDVELVETRPAGDGTF QKWAAVVVPSGEEQRYTCHVQHEGLPEPLMLRWKQ
>9RWI_3 Beta-2-microglobulin (chains B) IQRTPKIQVYSRHPAENGKSNFLNCYVSGFHPSDIEVDLLKNGERIEKVEHSDLSFSKDW SFYLLYYTEFTPTEKDEYACRVNHVTLSQPKIVKWDRDM
>9RWI_4 Fab heavy chain (chains H) QSVEESGGRLVTPGTPLTLTCTVSGIDLSSNAMSWVRQAPGEGLEWIGTISSGGRTYYAS WAKGRFTISKTSTTVDLKIPSPTTEDTATYFCGRGDGATGFNIWGPGTLVTVSSGQPKAP SVFPLAPCCGDTPSSTVTLGCLVKGYLPEPVTVTWNSGTLTNGVRTFPSVRQSSGLYSLS SVVSVTSSSQPVTCNVAHPATNTKVDKTVAPS
>9RWI_5 Fab light chain (chains L) ALVMTQTPASVSEPVGGTVTIKCQASQSIYSYLSWYQQKPGQPPKLLIYKASTLASGVSS RFKGSGSGTQFTLTISDLECGDAATYYCQNHWNVGGNGWPFGGGTEVVVKRTPVAPTVLI FPPAADQVATGTVTIVCVANKYYPDVTVTWEVDGTTQTTGIENSKTPQNSADCTYNLSST LTLTSTQYNSHKEYTCKVTQGTTSVVQSFNRGD
Preclinical characterisation and activity of a human leukocyte antigen-A (HLA-G) blocking antibody with enhanced Fc receptor-mediated effector function. O Dowd, V., McElhone, R., Thompson, C. et al. To be published.
Other PDB entries of the same protein (UniProt P16104 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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